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dnaJ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Length
403 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.251 kDa
Sequence
MKRDYYEILGVARSADKDEIKKAYRKLALKYHPDKNPDNKEAEEKFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGSGPGGAGYGDINDIFSAFNDMFSGGGGRARTGGSPFSGFEDVFSGGFSGSGSGRRRSAGIQGTDLKIRLKLTLEEIAKGVEKTIKIKKLVTCRECNGTGSKSGKTEICPTCHGSGEVRQATKTMFGQFMNISVCPTCGGEGRVVKDRCPSCYGEGIKQGEATVKITVPAGVQDGNYLTLQGQGNAGPRGGAPGDLIVVIEEKPHELFKRNGDDIIYDLSVGFPDLVMGTKIEVPTLDGHVKLTIPAGTQPNTMLRIGGKGIGHLRGGGSGDLYVRVNVFVPKEVSGKDRDLLKELKKSTVICPNHGDENHEKSIFEKAKDIFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
Length
401 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.913 kDa
Sequence
MKKDYYEVLGVSRSASKDEIKKAYRKLALQYHPDKNPDNKDAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGAGGAYAGGATDFNDIFSAFNDMFGGGRARGGGAPFGFEEVFGGGGGAGRRGRTSAGISGTDLKIRLKLTLEEIAKGVEKTLKIKKQIVCKECNGSGSKTGATEPCQTCHGSGEVRQASKTMFGQFVNITACPTCGGEGRVVKDRCTACYGEGIKQGDVTVKVTVPAGVQDGNYLTLRGQGNAGPRGGAPGDLIVVIEEKPHELFRRDGNDVIFNLALSYPDLVLGTKIDVPTLDGAVKLTIPPATQPESMLRIPGQGIGHLRGSGKGDQLVRVNVYVPKDLSHHEKELLKELKKTAAFSPSGSNNDKEEKSFFEKARDIFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobaculum parvum (strain NCIB 8327)
Length
401 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.765 kDa
Sequence
MKRDYYEILGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEKFKEANEAYEVLSNDDKRRRYDQFGHAGVGSSAASGGGPGGFGGGGYADINDIFEMFTGGGRARGGGSPFSGFEDIFGGGFSGGGGRRARSTGIHGTDLKIRLKLTLEEIAKGVEKTLKIKKQVVCSECNGTGSKSGKTETCQTCHGSGEVRQASKTMFGQFVNIVACPTCGGEGQVVKDRCTSCYGEGIKQGEVTVKINVPAGVQDGNYLTLQGQGNAGPRGGAPGDLIVIIEEKPHDQFKRNGDDIIYDLAVGFPDLVLGTKVDVPTLDGHVKLTVPAGTQPNTMLRIGGKGIGHLKGGGSGDLYVRVNVFVPKDVSGKDKEMLKELKKSSHISPNHGEQDHEKSIFEKAKDIFG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobium chlorochromatii (strain CaD3)
Length
400 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.881 kDa
Sequence
MKKDYYETLGVTRSSNKDDIKKAYRKLAVQYHPDKNPGNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGGGGAYAGGADFSDIFSAFNDMFTGGGARRGGSPFGGFEDAFGGGGGGGARRRASSGIHGTDLKIRLKLTLEEIAKGVEKTLKVKRQVPCEVCNGTGSKTGATETCQTCHGSGEVRQVSKTMFGQFVNIAACPTCGGEGRTIKERCTACYGEGIKLGETTVKINVPAGVENGNYMTMRGQGNAGPRGGAAGDLIVVFEEIHHETFTRNGHDVIYNLAVSYPDMVLGTKVEVPTLDGAVKLTIPAGTQPETMLRIQGHGIGHLKGGGRGDQYVKVNVFVPKEVSHQDKELLKDLRKSSNLCPNAHHDSESKSFFEKARDIFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
Length
396 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.159 kDa
Sequence
MKKDYYEILGVGRSADKDEIKKAYRKLALKYHPDKNPDNKDAEDHFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGGGAGAYGAGGADFSDIFSAFNDMFGGGGGGRGRGGFEDAFGGGQRRSRASAGIQGTDLKIRLKLSLEEIAKGVEKTLKIKKQVPCKECNGSGSKTGATETCPTCHGTGEVRQASKTMFGQFVNIAACPTCGGEGRIVKDRCPACYGEGIKQGEVTVKVTVPAGVQDNNYLTLRGQGNSGPRGGASGDLIVVIEEKPHEFFVRNGDDVIYSLAVSFPDLVLGTKVEVPTLDGAIKMTIPPSTQPETMLRIPGHGIGHLRGSGKGDQYVRVNVFVPKDLSATDKELLKGLRKSPGISPEAHGTGTEKSFFEKMKDIIG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Length
396 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.344 kDa
Sequence
MAEKRDYYEVLEVTKTATVEEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSNPDKRSRYDQFGHAGVSGAAGNGGPFGGFGGEGMSMDDIFSMFGDIFGGRGGGFSGGFGGFSGFGGGGGGSQQRRYRGSDLRVKVKMTLKEISTGVEKKFKLKKYVPCNHCHGTGAEGDGGSETCPTCKGSGSVIRNQQTILGTMQTRTTCPTCNGEGKIIKNKCKECGGDGIVYGEEVVTVKIPAGVAEGMQLSMGGKGNAGKHNGVPGDLLILVEEEPHPDLIRDENDLIYNLLLSFPTAALGGAVEIPTIDGKVKVKIDSGTQPGKVLRLRGKGLPNVNGYGTGDLLVNISIYVPEALNKEEKSTLEKMEASDNFKPSTSVKEKIFKKFKSFFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
Length
395 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.552 kDa
Sequence
MKRDYYEVLGVGRSATKDEIKKAYRKLAMKYHPDKNPDNSEAEEKFKEANEAYEVLSNDDKRRRYDQFGHAGVGSSASSQGGPFGGGGTGDLGDIFSAFNDMFGGGARGGGSPFGFEDVFSGGGGRRSRSAGVSGSDLKIRLKLSLEEIAKGVEKTLKIKKQVACDVCNGTGSKTGELETCPTCQGTGEVRQASKTMFGQFVNIAACPTCGGEGRVVKERCTACHGEGIKQGETTVKVNIPAGVEDGNYLTLRGQGNAGPRGGMNGDLIVVIEEVEHKIFARRGDDVVYNLTLSYADMVLGTKVDIPTLEGRVKMTVPPATQPNTVLRISAKGIGHLKAPGRGDHLVRVNVFVPKDPSHQDKELLKELNKSVHMVPDEKKEHEKGFYEKVKDIFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
Length
395 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.552 kDa
Sequence
MKRDYYEVLGVGRSATKDEIKKAYRKLAMKYHPDKNPDNSEAEEKFKEANEAYEVLSNDDKRRRYDQFGHAGVGSSASSQGGPFGGGGTGDLGDIFSAFNDMFGGGARGGGSPFGFEDVFSGGGGRRSRSAGVSGSDLKIRLKLSLEEIAKGVEKTLKIKKQVACDVCNGTGSKTGELETCPTCQGTGEVRQASKTMFGQFVNIAACPTCGGEGRVVKERCTACHGEGIKQGETTVKVNIPAGVEDGNYLTLRGQGNAGPRGGMNGDLIVVIEEVEHKIFARRGDDVVYNLTLSYADMVLGTKVDIPTLEGRVKMTVPPATQPNTVLRISAKGIGHLKAPGRGDHLVRVNVFVPKDPSHQDKELLKELNKSVHMVPDEKKEHEKGFYEKVKDIFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobium phaeobacteroides (strain DSM 266)
Length
395 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.537 kDa
Sequence
MKKDYYEVLGLSRSATKDEIKKAYRKLAMQYHPDKNPDNKDAEEHFKEVNEAYEALSNDDKRRRYDQFGHAGVGSSAASGGGQYGAGASDFSDIFSAFNDMFGGGKQRGGFEDVFGGAAGAGGRRGRASGGIHGTDLKIRLKLTLEEIAHGVEKTLKIKKQIACTECNGTGSKSGATETCPTCHGSGEVRQAAKTMFGQFVNITACPTCGGEGRVVKDRCVSCYGEGIKQGEVTVKVTVPAGVQDSNYLTLRGQGNAGPRGGANGDLIVVIEEKPHEKFQRNGDDVIYHLALGFPDLVLGTKVDVPTLDGSVKLTIPPSTQPETMLRIPGHGIGHLRGSGRGDQYVRVNVFVPKEVSSHDRELLKELKNSSAISPADQNDREEKSFFEKARDIFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Maricaulis maris (strain MCS10)
Length
395 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.542 kDa
Sequence
MSKRDFYEVLGVDKTADEKTLKSAYRKQAMKYHPDRNPGDAEAEAQFKVVGEAYSVLSDPNKRAAYDRMGHAAFEQGGGMGGGQGPFGGGGGAADFADIFEQVFGEAFNMGGGGGRRGGRGQAGPARGSDLRFDMEISLEDAFNGKDETIKVPTAMNCERCDGQGNEPGTELETCGTCQGAGRIRRSQGFFTMEQTCPQCGGRGQYVKTPCNDCDGVGRVRKTRTLNVTVPAGVEDGTRIRLAGEGEAGARGGPRGDLYIFISVREHEIFERDGPNLYCRTPASMVQAALGCTIQVPTIEGGKAEMKIAEGAQTGKRMRMRGKGMPRLRGGPRGDMIVELFVETPRNLCDRQKELLKEFCDLSGEGCNPDSAGFFNKVKQFWDEVTTDDGRPNAG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
Length
394 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.188 kDa
Sequence
MAEKRDYYEVLEVTKESTVEEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSNPDKRARYDQFGHAGMSGAAGNGGPFGGFSGGMSMDDIFSMFGDIFGGHSGGGFGGGFGGFGGFGGGGSQQRKFRGSDLRVKVKLNLKEISTGVEKKFKLKKYVPCSHCHGTGAEGNSGSETCPTCKGSGSVIRNQQTILGTMQTRTTCPTCNGEGKIIKDKCKVCGGEGIEYGEEVVTVKIPAGVAEGMQLSMGGKGNAGKHNGIPGDLLILVEEEPHPELIRDENDLVYNLLLSFPTAAIGGAVEIPTIDGKVKVKIEAGTQPGKVLRLRGKGLPSVNGYGTGDLLVNVSVYVPETLSKEEKSTLEKLEESKNFKPSTSIKEKIFKKFRSLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacteroides fragilis (strain YCH46)
Length
394 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.202 kDa
Sequence
MAEKRDYYEVLEVTKESTVEEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSNPDKRARYDQFGHAGMSGAAGNGGPFGGFSGGMSMDDIFSMFGDIFGGHSGGGFGGGFGGFGGFGGGGSQQRKFRGSDLRVKVKLNLKEISTGVEKKFKLKKYIPCSHCHGTGAEGNSGSETCPTCKGSGSVIRNQQTILGTMQTRTTCPTCNGEGKIIKDKCKVCGGEGIEYGEEVVTVKIPAGVAEGMQLSMGGKGNAGKHNGIPGDLLILVEEEPHPELIRDENDLVYNLLLSFPTAAIGGAVEIPTIDGKVKVKIEAGTQPGKVLRLRGKGLPSVNGYGTGDLLVNVSVYVPETLSKEEKSTLEKLEESKNFKPSTSIKEKIFKKFRSLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Fusobacterium nucleatum subsp. polymorphum
Length
394 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.153 kDa
Sequence
MAKRDYYEVLGVDKNASENDIKKAYRKAAMKYHPDKFANATDAEKKDAEEKFKEINEAYQVLSDNEKKQQYDQFGHAAFEQGGAGFGGGFNAGGFDFGDIFGDNIFGGGGGFGGFEGFSGFGGSSRRSYVEPGNDLRYNLEITLEEAAKGVEKTIKYKRTGKCEHCHGTGAEDDKMKTCPTCNGQGTIKTQQRTILGVMQSQSVCPDCHGTGKVPEKKCKHCRGTGTAKETVEKKINVPAGIDDGQKLKYAGLGEASQSGGPNGDLYIVIRIKPHDIFIRQGDNLYCEVPISYSTAVLGGEVEVPTLNGKKTVKVPEGTESGKLLKVSGEGIKSLKGYGKGDIIVKFTIETPKKLTDKQKELLQKFEESLNDKNYEQKTSFMKRLKKIFKDIID

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Synechococcus sp. (strain JA-3-3Ab)
Length
394 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.794 kDa
Sequence
MARDYYEILGVSRDSSKEEIKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDDELRARYDRFGEAGLSGAAAAASGFQDFAGIGGFADLFESFFTNFAGGGVGYSRSRQGPVRGDDLRFDLKLEFLEAIFGGEKQIRISHLEVCPVCGGSGAKPGTDVKVCPTCGGAGQVRRATRTPFGNFTQVSICPTCGGAGRVLEEPCYNCNGEGLAQTTKKLRINIPAGVDSGTRLRVSGEGDAGRRGGPPGDLYVYLFVEPDPDFQRDGLTIFSQVRVSYLQAILGAKVLVPTVDSKAGLEEEAELTIPAGSQPGTVLTLEGKGVPRLGNPMLRGDHKITLVVEIPTRISSEERELLMRLAELHGERINKRDGFLGGLLRGLAQMPGNREREEE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Synechococcus sp. (strain JA-2-3B'a(2-13))
Length
394 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.763 kDa
Sequence
MARDYYEILGVSRDSSKEEIKRAYRRLARKYHPDVNKEPGAEERFKEINRAYEVLSDNELKARYDRFGEAGLSGAAAAASGFQDFAGMGGFADIFESFFTNFAGAGASYARSRQGPVRGDDLRFDLKLEFLEAIFGGEKQIRISHLEVCNVCGGSGAKPGTEVKTCPTCGGSGQVRRATRTPFGNFTQVSVCPTCGGSGQVLEEPCYNCNGEGLAQTTKKLRINIPAGVDSGTRLRVSGEGDAGRRGGPPGDLYVYLFVEPDPDFQRDGLTILSEVRVSYLQAILGAKVSVPTVDSKAGLEEEVELTIPAGSQPGTVLTLEGKGVPRIGNPMSRGDHQITLVVEIPTRISSEERELLMRLAELHGERINKRDGFLGGLLRGLAQMPGNREREEE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia pneumoniae
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.109 kDa
Sequence
MDYYSILGISKTASAEEIKKAYRKLAVKYHPDKNPGDAAAEKRFKEVSEAYEVLSDPQKRDSYDRFGKDGPFAGAGGFGGAGGMGNMEDALRTFMGAFGGEFGGGSFFDGLFGGLGEAFGMRSDPAGARQGASKKVHINLTFEEAAHGVEKELVVSGYKSCETCSGQGAVNPQGIKSCERCKGSGQVVQSRGFFSMASTCPECGGEGRIITDPCSSCRGQGRVKDKRSVHVHIPAGVDSGMRLKMEGYGDAGQNGAPSGDLYVFIDVESHPVFERRGDDLILELPIGFVDAALGMKKEIPTLLKTEGSCRLTVPEGIQSGTILKVRNQGFPNVHGKGRGDLLVRISVETPQNLSEEQKELLRTFASTEKAENFPKKRSFLDKIKGFFSDFTV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.916 kDa
Sequence
MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSESSRQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGANTAKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSVCRGQGRIKDKRSVHVNIPAGVDSGMRLKMEGYGDAGQNGAPAGDLYVFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLSIPEGIQSGTVLKVRGQGFPNVHGKSRGDLLVRVSVETPQHLSNEQKDLLRQFAATEKAENFPKKRSFLDKIKGFFSDFAV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.916 kDa
Sequence
MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSESSRQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGANTAKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSVCRGQGRIKDKRSVHVNIPAGVDSGMRLKMEGYGDAGQNGAPAGDLYVFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLSIPEGIQSGTVLKVRGQGFPNVHGKSRGDLLVRVSVETPQHLSNEQKDLLRQFAATEKAENFPKKRSFLDKIKGFFSDFAV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.916 kDa
Sequence
MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSESSRQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGANTAKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSVCRGQGRIKDKRSVHVNIPAGVDSGMRLKMEGYGDAGQNGAPAGDLYVFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLSIPEGIQSGTVLKVRGQGFPNVHGKSRGDLLVRVSVETPQHLSNEQKDLLRQFAATEKAENFPKKRSFLDKIKGFFSDFAV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.916 kDa
Sequence
MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSESSRQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGANTAKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSVCRGQGRIKDKRSVHVNIPAGVDSGMRLKMEGYGDAGQNGAPAGDLYVFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLSIPEGIQSGTVLKVRGQGFPNVHGKSRGDLLVRVSVETPQHLSNEQKDLLRQFAATEKAENFPKKRSFLDKIKGFFSDFAV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.974 kDa
Sequence
MAKRDYYEVLGIDKSASENDIKKAYRKAAMKYHPDKFANASDAEKKDAEEKFKEINEAYQILSDSQKKQQYDQFGHAAFEQGGAGFGGGFNAGGFDFGDIFGDIFGGGGFGGFEGFSGFGGSSRRSYVEPGNDLRYNLEITLEEAAKGVEKTIKYKRTGKCENCHGTGGEDDKMKTCPTCNGQGTIRTQQRTILGVMQSQSVCPDCHGTGKVPEKKCKHCHGTGTAKETVEKKVNVPAGIDDGQKLKYAGLGEASQNGGPNGDLYVVIRIKSHDIFVRDGENLYCEVPISYSTAVLGGEVEIPTLNGKKMIKVPEGTESGKLLKVKGEGIKSLRGYGQGDIIVKITIETPKKLTDKQKELLQKFEESLNEKNYEQKSSFMKKVKKFFKDIID

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydophila caviae (strain GPIC)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.29 kDa
Sequence
MDYYDVLGVSKTASPEEIKKSYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDPQKRESYDRYGKNGPFAGAGGFGGMGGMGNMEDALRTFMGAFGGEFGGGGSFFEGLFGGLGEAFGMRGDPAGARQGASKKVHITLTFEEAARGVEKELLVSGYKTCETCLGSGAASEQGIKCCDRCKGSGQIVQSRGFFSMASTCPECGGEGRVITDPCSNCRGQGRIKDKRNVHVQIPAGVDSGMRLKMEGYGDAGQNGAPSGDLYVFIDVEAHPVFERRGDDLILELPIGFVDAALGMKKEIPTLLKEGMCRLTVPEGIQSGTILKVKNQGFPNVHGRGRGDLLVRVSVETPQNLSEEQKELLRKFATTEKAENFPKKRGFLDKIKGFFSDFAV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia muridarum (strain MoPn / Nigg)
Length
392 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.074 kDa
Sequence
MDYYTILGVAKTATPEEIKKAYRKLAVKYHPDKNPGDAEAERRFKEVSEAYEVLGDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGDFGGNGGGFFEGLFGGLGEAFGMRGGSEGARQGASKKVHITLSFEEAAKGVEKELLVSGYKSCDACSGSGAKTSKGVKVCDRCKGSGQVVQSRGFFSMASTCPDCSGEGRVITDPCSECRGQGRIKDKRSVHVNIPSGVDSGMRLKMEGYGDAGQNGAPAGDLYIFIDVEPHPVFERHGDDLVLELPIGFVDAALGIKKEIPTLLKEGTCRLNIPEGIQSGTVLKVRGQGFPNVHGKARGDLLVRISVETPQHLSNEQKELLRKFSETEKAENFPKKRSFLDKIKGFFSDFAV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Myxococcus xanthus
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.914 kDa
Sequence
MADDYYQTLGVDRSASAEDVKKAYRKLARKYHPDVNPGNKAAEEKFKQVSAAFEVLSDTRKRKLYDEFGPDAEKIGFDEKKAEAYRAYKASAGSAGAGGIPYGAEGFDLGDLFGDLFGGRGGGAAGGAPGGFDIGEMFGRRGRNAGPERGEDLTVRVQLTLAEAVSGTERPLAFNRPGRCSTCSGRGTSGPVSTCNVCNGTGRARRSGSLFGGAGACPNCHGTGKAAPPCPQCGGAGVKEELARLTVKIPAGVHTGSKVRLSGQGAAGTRGGPPGDLYIETEVAEHPLVRREGDDLHLDLPVTVSEALLGADVRVPTFQGEVTVKVLPHSQSGRRMRLKGRGVPSLKGGAQGDLYLHLQVKVPEETTAEARAAAEALARAYQGDVRRELTL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.391 kDa
Sequence
MATKTCYYEVLKVERTATKQQVDRAYRKLAIKYHPDSNRDDGSATAKFKEATEAYEVLSDANKRARYDQYGHAGVEGATQQYGDVEDIFEAFGDLFGGGFGDFFGGGSRRGGGRRRVRRGADVRCDVTLTLEEAARGCHKDIVFRRRVSCDTCDGSGAAAGSEPVTCTMCGGQGQVIQSAGILRVQTTCPTCKGAGKQIGEPCGKCRGTGTQNEKAEMNVEIPAGVDDGMRVRLQGEGEPSPDGGPNGDCYCFISVKEHNLFKREGQHLILQMPISYAQAALGATINVPTLDGPHELTVPAGTQTGHVFTVRGQGIVDPRSGRTGDLLVQIFIEVPKKLSDKQQKLLRELAELDHDSVLPERTSFLDKLRHFFDPEPEEAGTGSTDTEKDS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia abortus (strain DSM 27085 / S26/3)
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.072 kDa
Sequence
MDYYDVLGVSKTASPEEIKKSYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDPQKRESYDRYGKDGPFAGAGGFGGAGMSNMEDALRTFMGAFGGELGGSGSFFEGLFGGLGEAFGMRGDPAGARQGASKKVHITLTFEEAARGVKKELLVSGYKTCETCSGSGASSKQGIKCCDRCKGSGQVVQSRGFFSMASTCPECGGEGRMITDPCSSCRGQGRIKDKRSVHVQIPAGVDSGMRLKMEGYGDAGQNGAPAGDLYVFIDVEAHPVFERRGDDLILELPIGFVDAALGMKKEVPTLLKEGACRLTVPEGIQSGTILKIKNQGFPNVHGRGRGDLLVRVSVETPQNLSEEQKELLRKFAATEKAENFPKKRSFLDKIKGFFSDLTV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlamydia felis (strain Fe/C-56)
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.175 kDa
Sequence
MDYYDVLGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGPFAGAGGFGGAGMGNMEDALRTFMGAFGGEFGGGGSFFEGLFGGLGEAFGMRGDPAGARQGASKKVHITLTFEEAARGVEKELLVSGYKTCTTCSGSGAANERGIKCCERCKGSGQIVQSRGFFSMASTCPECGGEGRIITDPCSNCRGQGRVKDKRNVHVQIPAGVDSGMRLKMEGYGDAGQNGAPSGDLYVFIDVEPHPVFERRGDDLILELPIGFVDAALGMKKEIPTLLKEGTCRLTVPEGIQSGTILKVKNQGFPNVHGRGRGDLLVRVSVETPQNLSEEQKELLRKFSSTEKAENFPKKRGFLDKIKGFFSDFTV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
44.083 kDa
Sequence
MSSKRDYYEILEVSRSATQQDIKKAFRKLAMKYHPDRNKDSDAEEKFKEVNEAYEVLSDEEKRKLYDTYGHEGLNASGFHQGGFNPYDVFNSVFSGFDFEGGFGDVFSQFFGGGGSGFHNQEYIEEVDVNLVHEIKINFLEAANGCIKNVKYTRQVTCPDCNGSGSADGDVITCSDCNGEGFLVEQRRTLLGMFQTKKTCPSCKGEGQTIKNKCKKCKSRRMVDEVVERKVSIDSNVFYQDVVIVRGEGHIYKNLVGDLFLRVKIEPSRVFELRDNHVVVNVLVDPLVAITGGTILIPTLKEIKEINLKAGTKNGDIITIANGGINLKLDSRVYGANYNQKGDLIVVINYARPSEYSKQEITKLKEFIKPNKEVNLYETLMKKELNNKDSQ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.713 kDa
Sequence
MSEDFYDVLGVSRDATEDEIMQAYRDQVSEYHPDVSDDPDAEEKFKKIQKAKDVLTDEETRQQYDQLGHERFEEAEKRGATGNGGGGAGGMGGAGGPFGGGMGGGAGGGMGDIFEQFFGGAGGGGGRGRSGPEQGRDLRTDLTVTLSEAYRGVSKQVTVRRPESCADCGGSGYPEDADVRTCPQCDGQGVVTQVRQTPLGRVQQRQECSRCGGEGELHSETCSTCGGQGQTRERATLTVDIPEGIRTGQTLRMDGEGAPGEPGAPNGDLLVDVTVEEHPDFERDGDDLHHRHAVSFPQAVFGAEIEVPTLDGAATFDLDAGTQSGETFRLKGKGMPRLRRRGNGDLYVTVQVVTPESLSDEQRDALEQFAEAGGEEIDVEQGFFEKLKNSF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
Length
391 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.713 kDa
Sequence
MSEDFYDVLGVSRDATEDEIMQAYRDQVSEYHPDVSDDPDAEEKFKKIQKAKDVLTDEETRQQYDQLGHERFEEAEKRGATGNGGGGAGGMGGAGGPFGGGMGGGAGGGMGDIFEQFFGGAGGGGGRGRSGPEQGRDLRTDLTVTLSEAYRGVSKQVTVRRPESCADCGGSGYPEDADVRTCPQCDGQGVVTQVRQTPLGRVQQRQECSRCGGEGELHSETCSTCGGQGQTRERATLTVDIPEGIRTGQTLRMDGEGAPGEPGAPNGDLLVDVTVEEHPDFERDGDDLHHRHAVSFPQAVFGAEIEVPTLDGAATFDLDAGTQSGETFRLKGKGMPRLRRRGNGDLYVTVQVVTPESLSDEQRDALEQFAEAGGEEIDVEQGFFEKLKNSF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12)
Length
390 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
44.234 kDa
Sequence
MPTKKDYYEILGVPRNATQDEIKQAYRRLVRQYHPDLNKDPSAHEKFKEINEAYEVLSDPQKRAQYDQFGHVGDFSGYGDFQGGWQPGGFDFGDLGRNFEDIFENFFGDSIFGDLFGRRREREKAPRKGADLRYDINITLEEAAFGSEKEIYVTRLETCPTCKGKGTEPGTNPVKCDMCNGTGQIRNMRQTPFGQFVQITTCPKCHGTGQIIINPCHECHGTGKVRRKRRVEFKIPAGVDEGYVIRLAGEGEPGENGGPNGDIYIHIHIIPHKIFKRDNEDIWMELPIDYLIALLGGEVEVPTLEGKEKIYIKPGTQTGEVITLKGKGIPYLRNKNQRGDQKIVVKITVPQNLSPKEKELLLEIAKLRGINIEKDKNIFEQIKKAFKGDN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Length
390 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.167 kDa
Sequence
MAAGKRDYYEVLGVSRSATAQDIKRAFRKLAMQYHPDRHKGEGETVQKQNEEKFKEVNEAYEVLSDTEKRGMYDRFGHEGLNASGFHETGFNPFDIFNSVFGEGFSFDMDGGSPFDFIFSRGKKSRQNRVVLPYDLEIAVGVDISFFEMTNGCTRTIEYTKRVTCSACDGFGAEGGETGMVSCNSCEGNGFILKNQRSIFGTVQSQMLCQSCGGQGKQAKHKCKTCKGSKYKKVPTTKEIQIPAGIYHGDALVDDHGGNEFGGHVGKLVVHVGVLPSKIFKRVDHNVVANVLVDPMIAITGGKIELPTLEGIKEFNLRAGTKSGEQIVIPGGGIKFTKNFRKKAGDLIIIISYARPSEYSAPELRKLKEFIKPNQEVKQYLNALKNEYKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Length
389 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.99 kDa
Sequence
MATKRDYYEILGLSKDSSVEDIKKTYRKLALQYHPDRNKEPGAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYVTFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPNCGGTGQVRTTRSTLGMQFVSTTTCSACHGRGQVVESPCPTCSGAGRVRSRRKMSVNVPAGADSGMTLRLSGEGDAGEPGAPSGDLYIIVHVMEHKYFKRVDYDVISELPISFTQAALGADIMVDTLYGKVKMNIPSGTQTHSVFRLKDKGIQRLQGHGKGDQLVRVIIRTPTKLTQEQKDLLHQFEYLSNGKKPEAEERSRSDKQKSEKPRKSKGLFEKVKDAFES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methanosarcina mazei
Length
389 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.99 kDa
Sequence
MATKRDYYEILGLSKDSSVEDIKKTYRKLALQYHPDRNKEPGAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYVTFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPNCGGTGQVRTTRSTLGMQFVSTTTCSACHGRGQVVESPCPTCSGAGRVRSRRKMSVNVPAGADSGMTLRLSGEGDAGEPGAPSGDLYIIVHVMEHKYFKRVDYDVISELPISFTQAALGADIMVDTLYGKVKMNIPSGTQTHSVFRLKDKGIQRLQGHGKGDQLVRVIIRTPTKLTQEQKDLLHQFEYLSNGKKPEAEERSRSDKQKSEKPRKSKGLFEKVKDAFES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Length
389 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.746 kDa
Sequence
MAAGKRDYYEVLGISKNASSQDIKRAFRKLAMQYHPDRHKAENETTQKQNEEKFKEVNEAYEVLSDEEKRKLYDQFGHEGLNASGFHEAGFNPFDIFNSVFGEGFSFGMDGDSPFDFIFNRSKKRQQQIVVPYNLDIALVIEINFFEMTNGCNKTIKYERKVSCHSCNGFGAEGGESGLDLCKDCNGNGFVIKNQRSIFGTIQSQVLCSTCNGQGKQIKVKCKTCRSNKYTVTNQIKEINIPAGMYSGEALVDESGGNEFKGHYGKLIIQVNVLASKIFKRSDNNVIANVLVDPMVAIVGGVIELPTLEGIKEFNIRPGTKSGEQIVIPNGGIKFSKSFKRKAGDLIIIISYARPCEYTNLELKKLREFIKPNQEVKQYLNTLKNEYKT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.036 kDa
Sequence
MAQKKDYYEILGVPRNATEEEIKRAYRRLAKQYHPDANPGNKEAEEKFKEINEAYEVLSDPEKRKLYDQFGHAAFDPKYGAQGSGGFSGGFGGGFADFDFGSFGDIFEDLFEGFDIFGTSRRRKEAPRKGADIYVDLELTLKESVFGCEKEIPIYRTEKCSVCGGSGVKPGSAPVRCQKCGGTGQIRSRQATFFGEFTTIKTCDACGGTGTIITDPCRECGGTGNVRRQRRVKINIPAGIDDGQVITLRGEGESGIKGGPNGDLHIKIKIAPHPVFKRVGQDLYIEVPITFVNAALGGEIEIPTLDGKTKVRIEPGTQNGDEVRIKGKGVPNLRSRGRGDLVVKFIVEVPKKLTEKQKELLREFERLSSEEGYEKRKHFWDRIREAFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / JCM 1131 / NCIMB 11718 / AM63)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.859 kDa
Sequence
MAQRDYYDVLGVDKNASESDINKAYRKLAKKYHPDLNHEPGAEEKYKEVNEAYEVLHDKQKKAQYDQFGQAGVNGQAGFGGQGYGGFGGQGGYSSQGFGDFGDIFGDIFGSAFGGGRSRVDPTAPQKGQDLDYTMTIDFMDAIKGKKTDITYTRSEVCPTCDGSGAEKGTHPITCDKCHGTGVMTVTRQTPLGVIQQQTTCDKCGGRGTIIKHPCQTCHGKGTIDKKQTLEVKVPAGIDNGQQIRLSGQGEAGKNGGPYGDLYIVFRVKPSKEFRRNGTTIYSEAPISFAQAALGDKIRVNTVHGPVDLTIPAGTQPNTNFKLRGQGVPKINGTGNGDQEVTVKVVIPKKINDKQKEALVDYVKAGGGNISPQEKNFFERLKDKLNGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.803 kDa
Sequence
MAQRDYYDVLGVDKNASESEISKAYRKLAKKYHPDLNHEPGAEEKYKEVNEAYEVLHDKQKRAQYDQFGQAGVNGQGGFGGQGFGGFGGQGGYSSQGFGDFGDIFGDIFGSAFGGGRSRVDPTAPQKGQDLDYTMTIDFMDAIKGKKTDITYTRSEVCPTCDGSGAEKGTHPITCDKCHGSGVMTVTRQTPLGVIQQQTTCDKCGGRGTIIEHPCQTCHGQGTVDKKQTLQVTVPAGIDNGQQIRLSGQGEAGKNGGPYGDLYIVFRVKPSKEFRRNGTTIYTEAPISFAQAALGDKIRVNTVHGPVDLTIPAGTQPNTNFKLRGQGVPKINGTGNGDQEVTVKVVIPKKINDKQKEALVDYVKAGGGNISPQEKNFFERLKDKLNGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salinibacter ruber (strain DSM 13855 / M31)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.814 kDa
Sequence
MPRDYYDILGVDEDASDKEIKKAYRKKAMEYHPDRNPDDPEAEQKFKEASEAYEVLSDPEKRQRYDQFGHDGVDSGAGGGRRGRGRGFHDIEDIFDAFSDIFGGAPGGGRGRGRSERGRGRPGSDLRVSLSLTLEEIAEGTEKNLRLQKYLECESCDGTGAEGGMGGQNFSMCPKCDGTGEIRQVSRSVFGQVVNVQPCPRCEGEGRIIDNLCDDCGGEGRVQGEESISINVPPGVMEGNYLTLGDAGNAGLRGGPSGDLRIEIEEEPHEHFERDGLDIYYDLHLSFPEAALGTEVDVPTLEGEARLEVDPGVQAGKILRMRDRGLPDLEGSGQGDQMIRVHVWTPQELTAEEEELLDQLRAHDNFQPRPPEEDTQKSFFRRVSDVFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.526 kDa
Sequence
MSKRDYYEVLGVARTAGEGELKSAFRKLAMAYHPDRNPGDKEAEIKFKEVNEAYQTLSDGQKRAAYDRFGHAAFSQGAGGPGGPGFGADFGDFMSDIFDTFFGDARAGGAAGARGGRAGGRERGADLRYNLEITLEEAFTGKTETIRLPTSVTCEVCAGSGAKAGSKPRTCPTCGGYGRVRAAQGFFAIERTCPNCHGRGEIIDDPCTACGGAGRVTRERTLSVNVPAGVDDGLRIRLAGEGESGLRGGPAGDLYIFLSIKPHPFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSHTTVRIPAGTQTNKQFRLKGKGMPVLRSRDVGDLYIQVFVETPQNLTKRQRELLQEFDQHGSQADNHPESAGFFSRVKEFFDGLSGSGRA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma penetrans (strain HF-2)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.408 kDa
Sequence
MSSKRDYYEVLGVSKDATDDQIKSAFRKKAMQYHPDRNKEPDAEEKFKEVNQAYEVLSDPDKRANYDRFGHEGVDGQFGGGAGFDPFDIFNQFFGGGRGGGAHFEQSFGGSGFEDIFSNFFGGGRRGASSQQREANLVVSIVLTFVESVVGVKKTIEYKIEKDCESCHGSGADNSEGSISTCSNCNGSGVEITQKRTIMGIIQSQNICSRCNGEGKEIHKKCNSCKGRKVHEERVEIDVEIPGGVSNDEHLKVSGKGSVVGGKTGDLYINIQIKPSKIFSRKGNDIYVILKVDPILAIVGGEANIPTPFGIKSIKMKPGTRNGEIITVPSHGVKSTKRFGSNGDLFAVVEYTSAKRFSSAELKSLSKFAQETNDEIEKYLKEARKEIN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Buchnera aphidicola subsp. Cinara cedri (strain Cc)
Length
388 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.906 kDa
Sequence
MTKQDYYTTLNISNTASQLDIKRAYKKLAIKYHPDRNQGNKTAEEKFKKIKQAYEILSDTKKRNLYDQYGHSAFEQNNNSNNEFHSSFTTSTSDFNDIFGDVFGDIFGSNKKNRKEKGSDLQYNIILTLEEAVKGIKKEIRIPKLDKCQSCYGYGSAYGSKPSTCTSCNGHGQIHMRKGFFSVQQTCSTCRGTGTMIKNPCKICFGQGRIKKSKKLSITIPAGIDTNDQIRLNNEGEAGKYGAKSGDLYIQIKVKKHPIFKRDENNLHCKIPINFVIAGGSIILYSSFRGEITVPTLEGKINLKIPSETQSGKIFRIRGKGVKSVRKGFQGDLFCKIIVETPVNLNSFQKKILYQLGESFKNYKGENNSPKSKRFFNSVKKFFNNFTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium perfringens (strain 13 / Type A)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.877 kDa
Sequence
MAKRDYYEVLGLQKGASDDEIKRAFRKMAMKYHPDRNPGDKEAEENFKEVNEAYDVLKDPDKKAKYDQFGHAAFDGSGGFGGGGFGGFDAGGFDFSEMGGFGDIFESFFGGGFGGGSSRRRNAPQRGADLEYRLNITFEEAVFGCEKEISITRTENCETCHGTGAKAGTSPKTCPKCNGSGQIRVQRQTPLGSFVSTTTCDQCGGTGKVIEDPCPDCKGKGTVRKNRKITVKIPAGVDTGNIIPLRGQGEQGANNGPAGDLYIRVNVAPSKIFRREGSDIYYDYKISMAKAALGAEITVPTVDGNVKYKVPAGTQPGTKFRLKGKGVPHVNGGGRGNQYVHMVVEVPKHLNKEQEEALKAFMKASGESVDDIDEKDEGFFSKFKKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.878 kDa
Sequence
MAQKKDYYEILGVPRNATQEEIKRAYRRLAKQYHPDANPGNKEAEEKFKEINEAYEVLSDPEKRRKYDQFGHAAFDPTYGAQGGGFSGGFTGGFADFDFGSFGDIFEDLFEGFDIFGSSRRRKEAPRKGADIQVDLELTLKESVFGCEKEIPIYRTEKCSVCGGSGVRPGATPVRCQKCGGTGQIRSRQATFFGEFTTIKTCDACGGVGTIITDPCRECGGTGTVRRQRRVKINIPAGIDDGQVITLGGEGESGIKGGPNGDLHIRIKIAPHPVFKRVGQDLYVEVPITFVNAALGGEIEIPTLDGKTKIRVEPGTQNGDEVRIKGKGVPYLRGRGRGDLVVKFVIEVPKKLSEKQKELLRKFEELSSEEGYEKRKHFWDRIREAFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus casei (strain BL23)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.448 kDa
Sequence
MADQKDYYETLGVSRDADDDTIRKAFRKLSKKYHPDLNHAPGAEQKFKDINEAYQVLSDPQKRAAYDQYGSADGPQGFGGAGAGQGGFSDFGGGQGGFGGFDDIFSQFFGGAGGGAQANPSAPRQGADLQYRMDLTFEEAIFGKDTKISYDREAVCHTCNGSGAKPGTSPVTCHKCHGSGYIQVQRNTAFGAMMTRQVCDVCGGTGKEIKEKCPTCHGTGHEQERHTIDVKVPAGVEDGQQMRLQQAGEAGTNGGPYGDLYIVFRVAPSKKYQRDGSEIYLTIPLSFAQAALGDEIKVDTVHGAVELKIPAGTQSQTKFRLRGKGAPRLRGNGTGDQIVTVEVQTPKHLNEKQKSALMQFAAASGEDVTPHNGTLFDRVKEAFKGGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.448 kDa
Sequence
MADQKDYYETLGVSRDADDDTIRKAFRKLSKKYHPDLNHAPGAEQKFKDINEAYQVLSDPQKRAAYDQYGSADGPQGFGGAGAGQGGFSDFGGGQGGFGGFDDIFSQFFGGAGGGAQANPSAPRQGADLQYRMDLTFEEAIFGKDTKISYDREAVCHTCNGSGAKPGTSPVTCHKCHGSGYIQVQRNTAFGAMMTRQVCDVCGGTGKEIKEKCPTCHGTGHEQERHTIDVKVPAGVEDGQQMRLQQAGEAGTNGGPYGDLYIVFRVAPSKKYQRDGSEIYLTIPLSFAQAALGDEIKVDTVHGAVELKIPAGTQSQTKFRLRGKGAPRLRGNGTGDQIVTVEVQTPKHLNEKQKSALMQFAAASGEDVTPHNGTLFDRVKEAFKGGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacterium sp. (strain 4-46)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.403 kDa
Sequence
MSKRDYYEVLGVAKTAGEAELKSAFRKLAMAYHPDRNPGDKEAEIKFKEVNEAYQTLSDDQKRAAYDRFGHAAFSQGGPGGPGFGADFGDFMSDIFDTFFGDARAGGAGPRGGGGRAGGRERGADLRYNLEISLEEAFTGKTETIRLPTSVTCEVCAGSGAKAGSKPRVCPTCGGYGRVRAAQGFFAIERTCPNCQGRGEIIDDPCAACGGAGRVTRERTLSVNVPAGVDDGLRIRLAGEGESGLRGGPAGDLYIFLSIKPHPFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSHTTVRVPGGTQTNKQFRLKGKGMPVLRSRDVGDLYIQVFVETPQNLTKRQRELLQEFDQLGSQADNHPESAGFFSRVKEFFDGLSGSGRA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methanosarcina thermophila
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.554 kDa
Sequence
MATTRDYYEILGLSRDATPEDIKKSYRKLALKYHPDRNKEPGAEEKFKEISEAYAVLSDPEKRAQYDRFGHAGINGQYTAEDIFRGADFSGFGDIFEMFFGGSRRGPRGPRRGSDLQYDLYITFEEAAFGVRKDIDVPRTERCSNCSGTGARPGTSPKRCPTCGGTGQIRTTRTGLGMQFVSTTTCSTCRGKGQVIESPCPVCSGTGRVRNTRKITVNVPAGADSGMSLRLSGEGDAGDPGAPPGDLYVVLHVMEHKIFKRVDYDVISEVPISFAQAALGTDIMVDTLYGKVKMNIPAGTPTHSVFKIKEKGIQHLHGNRRGDQLVRVVIKTPTNLSHEQKRNFFASLKALSSGKNPGGEKGRYDKFTEKSKKSKGFFEKVKDAFES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.194 kDa
Sequence
MSEDFYDVLGVSRNADGDDIKQAYRKKAAKYHPDVSDDPNAEEKFKKIKKAKEVLTDGEKRQMYDQLGHDRFQQAEKRGGVGGGGNSSGGSARGDPFGGMGGQGSPFGDIFEQFFGGGQGQRRQGNRPRQGQNLQTRVQLDLEEVYTGVEKQFTVRRPEKCPDCNGRGHPSDADVRTCPQCNGQGQTTTVRETALGRVQQTQTCPRCDGSGEMYTQTCSTCNGDGVTRQEATLSVDIPAGIRDGQTLRMEREGAPGDNGGPRGDLLIDVSVRDHPDFERDGDDLYYRLAISFPQAVFGSTVEVPTVNGETTLDISAGTQSGEEFRIRNEGIPHLRGRGTGDLYVQVQIVTPENLSQKQREALEAFAEAGGESVDVSQGFFEKIKSSF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Hydrogenovibrio crunogenus (strain XCL-2)
Length
387 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.668 kDa
Sequence
MSKRDYYEILEVSATASEGEIKKAYRKLAMRYHPDRNPDDEEAEDKFKEASEAYEVLSDAQKRQAYDQFGHAGVDGSAGQGGFGGGGFADFGDIFGDIFGGGFGGGHRGPQPGSDLQYELEVSLEDAVAGTTVDVRIPTKELCESCDGSGAEPGSDVQTCPTCQGIGQVRVQQGFFAVSRTCPNCHGTGKLVKTPCKTCRGEGYKHSSKTLSVKIPAGVDNGDRIRLQGEGEAGEPGAPHGDLYVRIRVKEHKIFQRDGNTLFCDMPLSFATATLGGTMDVPTLNGKANLKIPAGTQSGQRFKLAGKGVKSVRSSHVGDMIVEVHIETPVKLTSEQKELLKAFDESLQGKHHKQHSPKTHSFFDSVKAFFKGDDEDGGNDKKDGPWN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Tetragenococcus halophilus
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.938 kDa
Sequence
MATKRDYYEVLGVDKGASDDEIKKAYRKLSKKYHPDVNQEADAEEKFKKFQKPMNTLSDPQKRAAYDQYGHAGADANFGGGGAGGFGGFGGGFSDAGGFGGFEDIFESFFGGGRSADPNAPRQGDDLQYSINLTFEEAVFGKDTEVSYKRNEVCHTCGGNGAKPGTQPETCHKCKGSGTINAERQTPLGRVMTRQTCDVCHGTGKEIKEVCETCHGTGHEKKTHSVNVSVPAGVEDGQQMRLANQGEAGTNGGPYGDLYVVLYCSHETCNIFDRDGSEIYYELPINFVQAALGDEVDVPTVHGNVKLKIPAGTQTSTKFRLRGKGAPRLRGNSTGDQQVTVKIITPKNLNEEQREALRNFAELTGQSTEEQQSEGFFDKMKDAFKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.087 kDa
Sequence
MAGKRDYYEILGVDRGASDAEIKKAYRKLAKQYHPDMNPGDKAAEAKFKEINEAYEVLSDPQKRARYDQFGHSAFDPNGFGGGGFGGGFTGGFGDFDFGGFGDIFEAFFGSGFGTRTSSARRGPQKGADLKYSMEVSFEEAAFGTEKEVTVSRLEICPTCSGSGTKPGHQPVTCRQCNGTGQVQYKQRTPFGQIVNVRTCDVCHGEGKIITNPCETCGGKGRVRKHTKLKVRIPAGIDNGETISLRGEGEHGIKGGPSGDLFITIKVKPHPIFKRHGNDVNCEIPITFTQAALGAEIEVPTLDGKEKIVIPEGTQTGTVFKLKGKGIPFLRSSGRGDQYVKVNIEVPRKLNEKQKEVLRQFAELVGDEVHEQRKGFFNKMKDALGM

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Protochlamydia amoebophila (strain UWE25)
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.058 kDa
Sequence
MADYYEILEVARGATPEEIKKAYRKKAVQYHPDKNPGDADAEKRFKEISEAYEVLSDEKKRQVYDRYGKEALQGAAGGGQGFSSMDEALRTFMGAFGMGGGGESIFDFFGGGNGAEFGGREGGRGARQGASKRVNINVSFEEAVKGVDKELVISNYANCNVCNGKGSSSSQGIKTCSECKGRGQVFEQRGFFSMTMACPKCHGEGKVITDPCKNCKGQGAVKEKQHIKVHIPAGVDSGMRLKMSGYGDVGQHGGPAGDLYVFINVEPHEIFEREGNDILLDLPISFAEAALGCKKEVPSLTNRACRITIPEGTQNGKIFRVKGEGFPNVHGHGKGDLLVRIFVETPTRLSERQKELLQEFSELEGPNNLPKRKGFLDKIKEFFSPN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Hyphomonas neptunium (strain ATCC 15444)
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.861 kDa
Sequence
MSKRDYYEVLGVERGVDEKALKSAYRKLAMKYHPDQNAGDTAAEDKFKEVGEAYAILSDPQKRAAYDRYGHGAFENGGMGGGSPFGGQGGNPEDIFQDLFSQVFGAGGFAGGRRRSGPQRGADLRYDLEITLEEAFYGKDETIHVPQAVACRPCEGTGAAPGTKPETCETCGGHGRVRAQQGFFTMERTCHICQGRGQIIRKPCKTCGGHGQVKEERKLQVKIPAGVESGMRIRLSGEGEPGTSGGPKGDLYIFVEVVEHDIFERDGPNLYCRAPVPMTTAALGGEIDIPTIDGGRARVAIPEGAQTGRKLRLRSKGMPSVRANGQTGDLYVEMFVETPQNLTARQKDLLRQFCDCSGADCHPESEGFLGKIKRFWGGEGDEKRPV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus fermentum (strain NBRC 3956 / LMG 18251)
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.865 kDa
Sequence
MAEEDLYDVLGVKKDASEAEIKRAYRKLAAKYHPDVNHEPGAEKKFKKINEAYETLSDDQKRAQYDQFGTTGSQAGGFGGQGGFGGFGQGGFSQGGFGDFSDIFGDIFGGGRARRDPSAPQQGRDLQYTMTLDFMDAVFGKETSIKYNRSAECHTCHGSGAKPGKSAHTCSTCHGQGYVLRQRQTMMGMMQSQEVCPTCGGKGQVIDPADQCDTCHGAGVTEERHELKVKVPQGIDDGQQMRLQGQGEAGKNGGPYGDLYIVFRVTPSRDFKRDGNTIYVDQDISISQATLGDHVQAKTVHGDVDLKIPAGTQSETKFRLRGKGVPRVNGNGNGDEYVTVHVKTPKTLNKRQREAMLAFAAASGEDVKGVKAGFFDKLKDAFEDNK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.541 kDa
Sequence
MDRLAKRDYYEILGVPRNATEAEIKKAFRNLARKYHPDANKDDPDAAEKFKEINEAYQVLSDPEKRARYDQFGHAAEQMGGAGGNPFEGFGGFGDFGGFSDIFEMFFGGAGRQRNPRGPVRGADLEYELELTLKEAAFGCTKELRVPRVEDCDTCHGSGARPGTQPVTCPKCGGTGQVQMTQHTVFGRFVNVMTCDRCRGEGKIVESPCPTCRGRGRVQKTQRVEVKVPGGVETGTRLRMPGYGEAGERGGPPGDLFIVMRVRPDRRFRREGDDLFTTTEISFIQAALGTEIEVETLDGPELIKIPEGTQPGDTIRLKGKGTHRLRGSGRGDLHVVISVKTPGRLSERERELLLEVAALRGERVAGMTENKEKSFLKKMKDALGGR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)
Length
386 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.924 kDa
Sequence
MSDNFYDVLGVSRDASEEEIKKAYRKQAAEHHPDVSDDDDAEERFKAIQKAKEVLTDEQKRQQYDQLGHDRFTEADKRGATGGGGPGGAGGPFGGAGGAGGAGGFEDIFNQFFGGGGGRGGGGGNRPRQGQDLRTGLTIDLEEAFEGATKEVTLTRPTQCDTCDGAGHPPDADVETCSQCNGRGQVQQVQQTPLGRVQQTSTCPRCEGSGELYSEDCADCGGDGVVREEATLSVEIPAGIRSGQSLRMEREGAPGENGGPNGDLLIEVDVDVGDRFERDGDDLRVNEAVSFPQAVFGDTIEVETVDGSVEMDVPTGTQSGETFRLKGKGMPRLRRRGRGDLYVKVGVVIPDSLNEEQREALEAFAEAGGEDVDVGGGFFKKLKSSF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.391 kDa
Sequence
MGKRDYYEVLGVGKTASEDEIKKAYRKLAMKHHPDRNQGDGAKASEEKFKEAKEAYEMLSDAQKRAAYDQFGHAGVDPNAGGAGFRPGAGGEGYGGFAEAFGDIFGDIFGQQGGGGRRGAGGQQVYRGADLSYAMEITLEEAAHGKESQIRIPTWEECDTCHGSGAKPGTSAKPCTTCHGAGTVHLRQGFFSIQQTCPHCHGSGKIIPEPCTSCNGAGKVKKQKTLEVKIPAGINEGQRIALRGHGEPGTQGGPAGDLYVEIRIKQHEIFERDSDDLHCTVPVPLTTAALGGAIEVPTLSGSAEIELPEGTQHGKTFRLRGKGIKGIRSNYPGDLYCHVSVETPVKLTEHQRKLLKELDESFRKGGDKHSPTSKSWTDRVKDLFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio harveyi
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.619 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKYHPDRNQGDESAADKFKEVKESYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGQQRAQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCDGSGAKKGSSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIRPCNECHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGERGEMGAPAGDLYVQVHVKEHHIFEREGNNLYCEVPVSFLMACSMAALGGEVEVPTLDGRVNLKVPTETRAGRMFRMRGKGVKGVRGGGVGDLIVKLVVETPVNLSARQKELLKEFDESCGGDAQLSTNQNLKGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio harveyi
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.619 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKYHPDRNQGDESAADKFKEVKESYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGQQRAQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCDGSGAKKGSSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIRPCNECHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGERGEMGAPAGDLYVQVHVKEHHIFEREGNNLYCEVPVSFLMACSMAALGGEVEVPTLDGRVNLKVPTETRAGRMFRMRGKGVKGVRGGGVGDLIVKLVVETPVNLSARQKELLKEFDESCGGDAQLSTNQNLKGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.433 kDa
Sequence
MSKRDFYDVLGVSRNASADELKKAYRSLAKKYHPDQNQGDKEAEQRFKELNEAYDALKDEQSRAAYDQFGHAAFDGGMGARGGPGGMGGFGAGASMSDIFDDLFGEFMGGRGGRGGRRGDGGQTRGHDLRYNMEISLEEAFEGKKAQVRVPGSVACEVCTGTGAAPGSSPITCPTCQGHGKVRASQGFFTIERTCPTCHGRGQTIDKPCTNCHGAGRVEKERTLSVNIPAGVEDGTRIRLSGEGEAGMRGGPAGDLYIFLSVKPHRLFERDGADLFCRVPIAMVTATLGGEIEVPTLGGKKVKVKVPEGAQTGRQFRLRGKGMPVVNSRETGDLYIQITVETPVNLTKKQKELLKEFEQASTPGNNPESAGFFAKVKEFWDGFQN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Jannaschia sp. (strain CCS1)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.093 kDa
Sequence
MAKRDYYEVLGVSKGASADEIKKGFRTKAKELHPDRNADNPEAESQFKEANEAYDVLKDADKKAAYDRFGHAAFDGGMAGGPRGGGGQGQGDFASAFSDVFEDLFGDFMGGQRGRPGGARTQATRGSDLRYNLSITLEDAYNGLSKQITVPSSVACSSCDGTGSEAGAEPTSCPTCSGMGKVRAQQGFFTVERTCPTCNGMGQIVKNPCRTCGGAGRQEKDRALSVNIPAGVETGTRIRLSGEGEAGLRGGPAGDLYIFVEVQDHALFQRDGMDLFCRVPVSMVSAALGGEIEVPSIDGGRSRVRVPEGSQSGRQMRLRGKGMPALRGPGLGEMYIELMVETPVNLTGDQAELLRQFEESCKKTNNPNASGFFDKVKSFWDKVRD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.965 kDa
Sequence
MRDYYEILGVTRTIDEAGLKSAFRKLAMEHHPDRNGGCENAAGRFKEINEAYSVLSDPQKRAAYDRFGHAGVNGPQGGPGGFGGQGFDASDIFNDVFGDVFGEMFGGGRRQSNAPQRGQDLRYDLEITLEQAYAGAEVEITVPAAMTCEVCEGSGAKPGTSPSVCGTCGGAGRVRATQGFFAVERGCPRCGGSGRLVLDPCSNCHGHGQVRRERILSVRIPAGVDDGARIRLAGEGDAGARGGPRGDLYIFLSVTPHELFERDGLDLLCTVPVPMTTAALGGEIDAPCLLGGESCDGECKVKVHVPEGAQTGKTVRLKGKGMPSLRSRQRGDLVVELFVETPTHLSARQKELMRELAGLCGEKQNPKSANFVGKAKRFWEEVTGS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacterium extorquens (strain PA1)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.347 kDa
Sequence
MSKRDYYEVLGVAKTASESELKVAFRKLAMVHHPDRNPGDKEAEIKFKEVNEAYQCLSDGQKRAAYDRFGHAAFSQGGAGGPGFGNEFGDFMSDIFENFFGDGRAAPGGGAGRGRGGAPGRERGSDLRYNLEISLEEAFAGKTETIRIPTSIACETCSGTGAKAGSKPRTCSTCGGYGRVRAAQGFFAIERTCPNCHGRGEVVDDPCTACSGAGRVNRERTLSINVPAGVDDGLRIRLAGEGESGMRGGPAGDLYVFLSIKPHPFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSQTQVRIPAGTQTGKQFRIKSKGMPVLRSREVGDLYIQVSVETPQNLTKRQRELLQEFDQSASDENHPESAGFFSKVRDFFVSGATRA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Halorhodospira halophila (strain DSM 244 / SL1)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.024 kDa
Sequence
MAKRDYYEVLGVNKNASDAEIKKAYRRMAQKFHPDRNPGDEESAERFKEVKEAYEVLSDAQKRAAYDQFGHAGVDPSAGGGPRGYGGGAGPGGPDFSDIFSDVFGDIFGSGGGRGGGRSRAFRGADLRYTLELSLEDAVRGTEEQIQVPTHVECDACKGSGSRAGSKPQTCPTCKGHGDVRVQQGFFSIQQTCPRCGGEGTMVTDPCPKCRGRGRVEDRKTLNVRIPAGVDTGDRIRLSGEGEPGERGGPPGDLYVQVAVREHEFFERDGADLHCQVPVDIVTAALGGEVEVPTLDGRVNLRIPPGTQPNQVFRLRGKGVKPVRGNRQGDLLCRIHVETPVNLTKRQRELLEEFQATLQDTGGKHHPHTSSWLDKVKRFIEEWRI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Helicobacter hepaticus (strain ATCC 51449 / 3B1)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.132 kDa
Sequence
METFDYYEILEITRTSDKETIKKAYRKMALKYHPDRNPDDKDAEEQFKRVNEAYEVLSDDSKRQIYDKYGKEGLQNSGFSGFSGRDFSDIFGDLGSIFESAFGANFGFSTQKRGGGKYNLDEIVGLELSFTEAVFGCKKEIHNSFKIACSDCKGTGAKGGKLNTCKDCGGKGQVYMRQGFMTFAQTCPTCKGEGQSASEKCSKCKGSGFEISEESFEVSIPEGIDDGNRIRIGGRGNADKNGSRGDLYIAVSVAEDENFVRDGENVYIEVPVFFTSIVLGTTLKIPSLRGELELKIPPNTRDKEQFVFDNEGIKDVNSAYRGKFVAQIKITYPPKLNAEQRALTEKLQESFGIESEPYKNVFEECFTKVKQWLHKHSKNDKDTTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Ruegeria sp. (strain TM1040)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.096 kDa
Sequence
MSKRDYYEVLGVSKGASADEIKKGFRKKAKELHPDRNADNPDAEAQFKEANEAYDVLKDPERKAAYDRYGHAAFENGMGGGGGGRAGGHPGGDFSSAFSDVFDDLFGDFMGGGGGRAGARQRATRGADLRYNLRLSLEEAFAGLHKTINVPTSVSCTSCEGTGAEGGAEPTTCPTCSGMGKVRAQQGFFTVERTCPTCSGLGQMIKNPCKTCNGHGRVEKDRSLSVNIPAGVETGTRIRLAGEGEAGLRGGPPGDLYIFIEVARHELFEREGNNLHCRVPVSMAKAALGGAIEVPTIDGGRGRVQIPEGSQSGRQMRLRGKGMPALRGGGTGDMFIELAVETPVNLTPRQKEILKEFDEISEENTNPETRSFFSSVKSFWDGMKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.156 kDa
Sequence
MAKRDYYEVLGVAKNASDEDLKKAYRKLAMKYHPDRNPDSKEAEEKFKEAKEAYEVLGDEQKRAAYDRYGHAGVDPNAAGMGGGMGGGMGGGMGGGMGGGFADAFGDIFGEIFGAGRRGGGGPQVYRGADLKYALEITLEQAASGFDTEIRVPSWENCDTCHGSGAKAGTSPKTCRTCGGSGAVRMQQGFFSVQQTCPTCHGTGKEITDPCPSCDGVGRTRRNKTLQVKIPAGIDDGMRIRSSGNGEPGINGGPPGDLYVEIHIKQHKIFQRDGDDLHCELTIPFTTAALGGELQVPTLGGKAEISIPEGTQSGKTFRLRAKGIRGVRGSYPGDLYCHVVVETPVRLSDEQKAILRQFEASLNDGGDRHSPQSKSWTDRVKEFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacterium extorquens (strain CM4 / NCIMB 13688)
Length
385 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.351 kDa
Sequence
MSKRDYYEVLGVAKTASESELKVAFRKLAMVHHPDRNPGDKEAEIKFKEVNEAYQCLSDGQKRAAYDRFGHAAFSQGGAGGPGFGNEFGDFMSDIFENFFGDGRAAPGGGAGRGRGGAPGRERGSDLRYNLEISLEEAFAGKTETIRIPTSIACETCSGTGAKAGSKPRTCSTCGGYGRVRAAQGFFAIERTCPNCHGRGEVVDDPCTACSGAGRVNRERTLSINVPAGVDDGLRIRLAGEGESGMRGGTAGDLYVFLSIKPHPFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSQTQVRIPAGTQTGKQFRIKSKGMPVLRSREVGDLYIQVSVETPQNLTKRQRELLQEFDQSASDENHPESAGFFSKVRDFFVSGATRA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Paracoccus denitrificans (strain Pd 1222)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.171 kDa
Sequence
MAKRDYYEVLGVARGASADEIKKAYRAKAKQLHPDRNKDCKVSEAAFKEVNEAYECLKDDQKKAAYDRFGHAAFENGGGGFGRGNGHGDFGSAFADVFEDLFGDMMGRRAGGGGRSRASRGQDLRYNLRVSLEEAYNGAQKTINVPGSVACAACNGTGAEGAVEPATCPTCSGMGKVRATQGFFTVERTCPTCSGHGQIVKNPCQECRGAGRVQKERTLSVNIPAGVETGTRIRLAGEGDAGMRGGPAGDLYIFIEVREHPIFMRDGRMLACQVPVSMTTAALGGEIEVPTIDGGRSRVKVPPGTQSGKQLRLRGKGMPPLRHGPGLNGEAGDMLIELAVETPVNLTARQKELLREFEAINADNNPQTQGFFQKIKGFWDEMKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Peptoclostridium difficile (strain 630)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.071 kDa
Sequence
MSTKRDYYEVLGISKGAEAQEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEINEAYEVLSDDTKRKTYDQFGHDGLNGQGGFGGQGGFGGQGFGGFEDMFGDIFGDMFGGSFGGGRARRRGPQRGADIRQSVTISFEEAAFGKKMSIKVNRSEECEECNGTGAKPGTSKKTCSTCNGTGQVRTVQRTPFGNIASSRPCSACNGTGEVIESPCSKCHGTGNTRKVKTIEVDIPAGIDDGQMIKLSGQGEVGEKGAPRGDLYIVVNVKSHPLFTRDGNDIYFEMPITFVQATLGDEIEVPTLDGKVKYSVPEGTQTGTVFRLKEKGIPRIRGNSRGDQYVKVVVEIPKKLNDKQKELLREFAKECGSNVHEKKKTFGQKIEDMFKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodobacter capsulatus
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.692 kDa
Sequence
MAKVDFYEVLGVSKGASAEEIKKAYRSKAKELHPDRNQGQSAAEAQFKEVNGAYDVLKDGDKKAAYDRYGHAAFEGGMGGGGPRGPYGQGADFSSAFSDVFEDLFGDFMGGRGGPGGGGRRVRRRGSDLRYNMRVTLEEAFKGAQKTITVPGSAACGSCNGTGAEGGAEPQTCPTCSGLGKVRAQNGFFTVERTCPTCGGQGQVVKNPCRVCHGSGRIEKERTLSVNIPAGVETGTRIRLAGEGEAGMRGGPSGDLYIFIEVREHAIFQRDGVNLFCRVPVSMVSAALGGEVEVPTIDGGRSKVKVPVGSQSGRQMRLRGKGMPALRGGGIGDMVIELAVETPVNLTARQKELLDEFQRIQAENNPEGASFFQKVKSFWDGMKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.718 kDa
Sequence
MPKKDLYEILGVDRNASQEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFEQGGSQQGGFGDFGEGGFDFDFGGFGDIFGDIFSDFFGTGRRKAEKGPKKGADIRYDLTLTFEEAAFGTEKEIEVERFEVCDVCHGTGVKPGSRPETCPVCHGTGEIRQTQNTPFGRIVNIRTCPRCHGEGKIITDPCQKCGGTGKIRKRRKIKVTIPAGIDEGQMLTLRGEGEPGLRGGPNGDLYIVIHVKPHEIFKREGYDVYVKIPISFADAALGGEIKIPTLDGMVSFTIPEGTQTGTKFKLRGKGIPHIGGRGRGDQIVEVYVEVPKRLSEKQKELLREFKRLEGENTAEHKSFFQRMRDAFGGS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.243 kDa
Sequence
MATQDFYQVLGVSKDANERDIKKAYKRMAMKYHPDRTEGDKDMEIKFKEIKQAYEVLSDPQKRQMYDQYGHEAFEQARQGGAGHGAGGFGGGGADFADIFGDVFGDIFGGGRRQQARAQRGADLRYNLDMSLEEAVRGKTVELEIPTLVECRDCNGSGAKKGSKPQTCGHCHGSGQIQMRQGFFAVQQTCPQCRGTGTIIKDPCRTCHGHGRKEETKTLSVKIPAGVDTGDRIRLANEGEAGEHGAPAGDLYVQVHVREHPIFARDGNNLFCEVPVSFTKAALGGDIEVPTLEGKVKLKVPKETQTGKHFRLRGKGVKSVRTGEVGDLICKVMIETPVNLSSKQRDMLEELEDSMGTGDEAAKFRPKEKGFFDGVKQFFDDLRS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.027 kDa
Sequence
MAQEDYYKVLGVDRDASDQEISKAYRKLAKKYHPDLNHEPGAEEKYKQVNEAYEVLHDKQKRAQYDQFGSAGVNGQGGFGGAGQGFGGAGFDTSGFGDFGDIFGDIFGQGARQQRVDPTQPQRGQDLDYTLTIDFMDAINGKKTQVSYTRDETCETCGGNGCEKGTHPITCDKCHGTGVMTVTQQSMLGMIRRQTTCDKCNGRGVIIEHPCKTCGGKGTVERKNTIEVDIPAGIDNGQQLRYQGQGEAGRNGGPYGDLYISYRIKPSKDFERRGQNIYTEVPISFAQATLGDEITVKTVHGDAKLTIPAGTQPNKKFTLRGQGVPYLRGNGNGDQITTVNIVIPKHINDKQKEDLTNFVHDGGGNITPQEKGFFERLKDKLSGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.927 kDa
Sequence
MGKRDYYEILGVTRQASEEEIKKAYRKLALKYHPDRNPGDKDSEELFKEAAEAYEVLHDAQKKRIYDTYGHEGLRGTGFSGFRGFEDIFSSFGDVFQEFFNFGFGAGGQSRTAARPGDDLLYDLSLTFEEAVFGTEKEIRLQTLTTCEECNGSGAEPGTRETVCPVCQGSGQVVQSQGFFRISATCTRCQGMGKVLVSPCKTCNGQGRTRQSKTVQVRVPAGVDTGTRLRLRGEGESGYRGGVAGDLYVRLHVNPHEFFERDGDNLYCKVSVSFAQAILGDQIEIPTLDGGRELKIQPGTQPGAVIRFSGEGVPRLRGYGRGDLFIEVEVKIPTRITPRQEEIVTEFMQIEKEKSGEKVRKWPWSKRKDREKKSMAESTREART

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.752 kDa
Sequence
MSQDFYEILGVSRDASEDEIQEAYREKAREYHPDVSDDPDAEEKFKQAKKAKEVLTDEEKRQMYDQMGHERFEQAEKRGGAGGGGGRGGMGGDPFGGGAGGFDMQDIFDQFFGGGGRGGRGGSRRRQGQDLQTRLEIDLEEAYNGATKQLNVTRPEACDDCDGAGHPPGADSETCPECNGQGQTTQVQQTPMGRVQQRTTCRRCDGEGTLYDETCSTCRGNGVVQNDASLEVEIPSGIADGQTLRMEREGAPGENGGPNGDLLIEVQVRDHPDFERDGDSLQHQQAISFPQAVFGDTITVPTLDGEVEVDVPSGTQSGEVFRLEGKGMPRLRRRGHGDLYVQVQVVTPDSLNAEQKEALEQFAEAGGEEVDVDEGFFEKLKNSL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.783 kDa
Sequence
MSEDFYDVLGVSRDASKDQIKNAYRKKAAKYHPDVSDEEDAEEKFKKVQKAKEVLTDDEKRQMYDQLGHERFQQAQKRGAGGGGGGRGQGNPFGGGGNPFGGMGGGGFEDIFNNLFNGGGGQRRSRPQQGRDVAQRITIDLEDAYHGVERDVTIRRREVCPECDGEGHPADADVNTCSECNGSGQQTTVQQTPFGRVQQTTTCRACGGEGKTYSEDCSECRGSGRVRRTRDVTITIPAGFRDGQRLRYRGEGEPGENGGPNGDLFVEVNVRDHEEFDRDGDDLQYTHPISFPQAVFGATVEVPTLDGEAELKVPAGTQSGSTFTVSGAGMPHLDGRGNGDLHVEIHVVTPEDLNSEQREALKQFAEAGGEEVKESLFQKLKNSL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Roseobacter denitrificans (strain ATCC 33942 / OCh 114)
Length
384 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.602 kDa
Sequence
MAKRDYYEVLGVSKGASSDDIKKGYRRKAKELHPDRNKDDPNAEAQFKEANEAYEVLKDADKKAAYDRYGHAAFEGGMGGGGGGRPGGGFGGGQDFSSAFSDVFDDLFGNFAGGGQRGGGNRASRGSDLRYNLQINLEDAFSGLQKTINVPTSIGCKTCNGSGAEGGSEPSSCPTCSGMGKVRAQQGFFTVERTCPTCSGLGQIIKNPCKSCQGAGRVEKDRALSVNIPAGVETGTRIRLAGEGEAGMRGGPSGDLYIFIEVAEHELFQRDGTNLFCRVPVSMAKAALGGSIEVPTIDGGRGRVQIPSGSQSGRQMRLRGKGMPALRGGSSGDMFIELAVETPVNLTSRQKELLAEFDELSENNNPESSSFFSSVKSFWDSMKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus reuteri (strain DSM 20016)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.63 kDa
Sequence
MAEQDYYDILGVSKDASEKDIKRAYRRLAAKYHPDVNHEPGAEEKFKKINEAYETLSDSQKRAQYDQFGSAGPQGAGGQGFGGFGGGQAYSNFGGGFDDIFSQFFGGGGRTRRDPTAPRQGRDLQYAMTLDFMDAVFGKTTTIKYDRDAECKTCHGTGAKPGKSPITCPRCHGAGVITSVRQTPLGNMQTQTTCPECNGTGKIIKPEDRCDTCHGAGHVHERHELEVKVPAGVDDGQQMRLQHQGDAGENGGPAGDLYIVFRVTPSREFRRDGSTIYVDRDISFAQAALGDEVKVKTVHGDVNLKIPAGTQSETNFRLRGKGVPHLNGNGNGDEHVTVHVKTPKSLNKRQREAMLAFAAASGEDVKGVKKTVLDKLRDAFEDK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus reuteri (strain JCM 1112)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.63 kDa
Sequence
MAEQDYYDILGVSKDASEKDIKRAYRRLAAKYHPDVNHEPGAEEKFKKINEAYETLSDSQKRAQYDQFGSAGPQGAGGQGFGGFGGGQAYSNFGGGFDDIFSQFFGGGGRTRRDPTAPRQGRDLQYAMTLDFMDAVFGKTTTIKYDRDAECKTCHGTGAKPGKSPITCPRCHGAGVITSVRQTPLGNMQTQTTCPECNGTGKIIKPEDRCDTCHGAGHVHERHELEVKVPAGVDDGQQMRLQHQGDAGENGGPAGDLYIVFRVTPSREFRRDGSTIYVDRDISFAQAALGDEVKVKTVHGDVNLKIPAGTQSETNFRLRGKGVPHLNGNGNGDEHVTVHVKTPKSLNKRQREAMLAFAAASGEDVKGVKKTVLDKLRDAFEDK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus sakei
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.132 kDa
Sequence
MAEKRDYYDVLGVGRDASDDEIKKAYRKLSKKYHPDINKAPDAEAKFKEVTEAYEALSDPQKRAAYDQYGHAGMNGGFGGGAGAGQGFGGFGGGAEGFGGFDDIFSSFFGGGARQQPNGPRQGSDLQYRMDLKFEEAVFGKETKISYSREAECHTCHGSGAKPGTSAETCHKCHGAGQIQVERQTPLGRMMSRETCDVCGGTGKEIKSKCDTCHGTGREEERHTVKVKVPAGVEDGQQMRLQGQGEAGSNGGPYGDLFIVFRVAPSDEFERDGAQIFVEVPISFVQAALGDEIEVNTVHGPVKLKIPAGTQTNTVFRLRGKGAPKLHGTGNGDQKVTVNVVTPKSLNSKQRDALKAFAVASGDSVNPQDNNLFDKILNKKHKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus sakei subsp. sakei (strain 23K)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.131 kDa
Sequence
MAEKRDYYDVLGVGRDASDDEIKKAYRKLSKKYHPDINKAPDAEAKFKEVTEAYEALSDPQKRAAYDQYGHAGMNGGFGGGAGAGQGFGGFGGGAEGFGGFDDIFSSFFGGGARQQPNGPRQGSDLQYRMDLKFEEAVFGKETKISYSREAECHTCHGSGAKPGTSAETCHKCHGAGQIQVERQTPLGRMMSRETCDVCGGTGKEIKSKCDTCHGTGREEERHTVKVKVPAGVEDGQQMRLQGQGEAGSNGGPYGDLFIVFRVAPSDEFERDGAQIFVEVPISFVQAALGDEIEVNTVHGPVKLKIPAGTQTNTVFRLRGKGAPKLHGTGNGDQNVTVNVVTPKTLNSKQRDALKAFAVASGDSVNPQDSNLFDKILNKKYKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.135 kDa
Sequence
MAEKRDYYEVLGVSKNATDDELKKAYRKKAIQYHPDKNPGDKEAEEHFKEVAEAYDVLSDPEKRSRYDQFGHAGLGGAAGGGFSGGGMSMEDIFSRFGDLFGGFGGFGGFSDMGGSSRRRVRRGSDLRVRVKLSLADISKGVEKKVKVKKQVVCSKCRGDGTEEANGKTTCQTCHGTGVVTRVSNTFLGAMQTQSTCPTCHGEGEIITKPCSKCKGEGVEIGEEVISFHIPAGVAEGMQMSVNGKGNAAPRGGVNGDLIVVIAEEPDPNLIRNGNDLIYNLLISVPLAIKGGSVEVPTIDGRAKIRIEAGTQPGKMLRLRNKGLPSVNGYGTGDQLVNVNVYIPESIDAKDEQAIAAMENSDSFKPTDAARKDIDKKYREMLD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.106 kDa
Sequence
MAEKRDYYEVLGVSKNATDDELKKAYRKKAIQYHPDKNPGDKEAEEHFKEVAEAYDVLSDPQKRSQYDQFGHAGLGGAAGGGFSGGGMSMEDIFSRFGDLFGGFGGFGGFSDMGGGSRRRVRRGSDLRVRVKLSLADISKGVEKKVKVKKQVVCSKCRGDGTEEANGKTTCQTCHGTGVVTRVSNTFLGAMQTQSTCPTCHGEGEIITKPCSKCKGEGVEIGEEVISFHIPAGVAEGMQMSVNGKGNAAPRGGVNGDLIVVIAEEPDPNLIRNGNDLIYNLLISVPLAIKGGSVEVPTIDGRAKIRIEAGTQPGKMLRLRNKGLPSVNGYGMGDQLVNVNVYIPESIDAKDEQAIAAMENSDSFKPTDAARKDIDKKYREMLD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.135 kDa
Sequence
MAEKRDYYEVLGVSKNATDDELKKAYRKKAIQYHPDKNPGDKEAEEHFKEVAEAYDVLSDPEKRSRYDQFGHAGLGGAAGGGFSGGGMSMEDIFSRFGDLFGGFGGFGGFSDMGGSSRRRVRRGSDLRVRVKLSLADISKGVEKKVKVKKQVVCSKCRGDGTEEANGKTTCQTCHGTGVVTRVSNTFLGAMQTQSTCPTCHGEGEIITKPCSKCKGEGVEIGEEVISFHIPAGVAEGMQMSVNGKGNAAPRGGVNGDLIVVIAEEPDPNLIRNGNDLIYNLLISVPLAIKGGSVEVPTIDGRAKIRIEAGTQPGKMLRLRNKGLPSVNGYGTGDQLVNVNVYIPESIDAKDEQAIAAMENSDSFKPTDAARKDIDKKYREMLD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.106 kDa
Sequence
MAEKRDYYEVLGVSKNATDDELKKAYRKKAIQYHPDKNPGDKEAEEHFKEVAEAYDVLSDPQKRSQYDQFGHAGLGGAAGGGFSGGGMSMEDIFSRFGDLFGGFGGFGGFSDMGGGSRRRVRRGSDLRVRVKLSLADISKGVEKKVKVKKQVVCSKCRGDGTEEANGKTTCQTCHGTGVVTRVSNTFLGAMQTQSTCPTCHGEGEIITKPCSKCKGEGVEIGEEVISFHIPAGVAEGMQMSVNGKGNAAPRGGVNGDLIVVIAEEPDPNLIRNGNDLIYNLLISVPLAIKGGSVEVPTIDGRAKIRIEAGTQPGKMLRLRNKGLPSVNGYGMGDQLVNVNVYIPESIDAKDEQAIAAMENSDSFKPTDAARKDIDKKYREMLD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.203 kDa
Sequence
MAKRDYYDVLGVSKGASPDEIKKGFRKKAKELHPDRNSDNPNAEAQFKEANEAYDILKDPDKKAAYDRYGHAAFENGSGGPRGPGGFGGQGQGDFASAFSDVFEDLFGDFMGGQRGGGRQRAARGSDLRYNLRITLEQAFMGMQKTISVPGTVSCSACEGTGAEGGAEPVVCPTCSGMGKVRAQQGFFTIEKTCPTCSGMGQIIKNPCQACRGAGREEKTRALSVNIPAGVETGTRIRLAGEGDAGVRGGPSGDLYIFIEVEEHRIFQREGLDLYCRVPVSMTSAALGGDVEVPTIEGGRSRVKIPSGSQSGRQMRLRGKGMPALRGAGTGDMFIELAVETPVNLTMRQRELLREFEAESQDNQPETSKFFKTVKSFWDGMKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.392 kDa
Sequence
MSKSDYYEALGVARNASDSEIKKAYRRMAMKYHPDRNPGDKEAEARFKEAKEAYEILSDPQKRAAYDQFGHAGVDPSAGMGGAGGPGGPGGPDFADIFSDVFGDIFGGGGRRGGGGRRVFRGADLRYNLELSLEDAVRGTEVQIRVPTQEVCDACDGKGTKEGSQPETCPTCKGHGDVRIQQGFFSVQQTCPRCGGSGSVITDPCRKCGGRGRVQSQKTLSVRVPAGVDTGDRIRLSGEGEPGENGGPPGDLYVQIMVREHEFFQRDGANLRCEVPISITKAALGGEVEVPTLDGRVNLRIPAGAQSGKVFRVRGKGVKPVRGGPQGDLLCRVHVETPVNLTKKQKELLEEFGRTMDDTGDKHTPRTSSWLDKARKFFEDWKL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.13 kDa
Sequence
MARDLYETLNVSRDASKEDIKRAYRKLARQYHPDVNKDAGAEDTFKELSRAYEVLSDDDQRARYDRFGEAGLNGGVGGGPGDFAGAAGFGDISDIFESFFGGFAGAGTGGRRATRPGGPTRGDDLRYDMVLEFQEAIFGGEKEITINHLITCETCRGSGSKPGSGPMTCRNCGGQGQIRQARRTPFGLFTQVAACPNCQGTGEVIESPCPTCSGRGRNQKQTTIKITIPAGVDAGSRLRVQGEGDAGMRGGPPGDLFIYVSVRNHPVFRREGQDIYSIAEISYLQAILGSQMSVETVDGPQTVVVPPGTQPETVLTLDGKGVPRIGNPTRRGNHYLQLKVVIPTKLGAEERELLTKLAKARGEKVSKKEGLEGLIDSIGNLFH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.158 kDa
Sequence
MSKRDYYEVLGVAKTASESELKVAFRKLAMVHHPDRNPGDKEAEIKFKEVNEAYQCLSDGEKRAAYDRFGHAAFSQGGAGGPGFGNEFGDFMSDIFENFFGDGRGAPGGGRGRGGAPGRERGADLRYNLEISLEEAFSGKTETIRIPTSIACEACSGTGAKAGSKPRTCSTCGGYGRVRAAQGFFAIERTCPNCHGRGEVVDDPCTACSGAGRVNRERTLSINVPAGVDDGLRIRLAGEGESGLRGGPSGDLYVFLSIKPHPFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSQTQVRIPAGTQTAKQFRIKGKGMPVLRSREVGDLYIQVSVETPQNLTKRQRELLQEFDQSASDENHPESAGFFSKVRDFFVSGATRA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
43.299 kDa
Sequence
MSKQDYYKTLGVTQSSDEREIKRAYKKLAMKYHPDRNPGNKNSEEKFKTIKEAYEILIDPKKRTAYDQYGHSAFEQGNSTGNNNTFTHSFSSNSDFSDIFGDVFGDIFGGTRKQKSERQGSDLRYDMTLTLEEAVRGTIKEIKIPTLQKCPTCYGYGTKTGTKPQFCPTCRGNGQIQMRKGFFTVQQTCPQCHGEGNFIRDPCRRCHGNGRIEISKTLSVKVPPGVDTNDKIRLNNEGEAGENGAMAGNLYVQINVKKHPIFEREENNLYCEVPISFSMAALGGEIEVPTLDGKVKLKIPCETQSGKLLRIRGRGVKSIRNNNRQGDLLCRIIVETPVNLNDLQKDLLYKLGESFNGFKGEKNSPKSKRFFEGVKRFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Length
383 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.046 kDa
Sequence
MSKQDYYELLGVEKGASPDDIKKAYRKQAMQFHPDRNPGNADAEQKFKEINEAYDVLKDEQKRAAYDRFGHAAFEQGGPGGGGGGGFGGFGGGGFSDIFDEMFGEFMGGGGRRGQSTGRGADLRYNMDISLEDAFAGKTATVKVPSSAPCEDCKGTGGKDGAQPVTCSACHGHGKVRQQQGFFTIERTCPTCQGMGKIIKDPCRSCGGSGRTRKEKTLQVNIPAGVEDGTRIRLAGEGEAGMRGAPAGDLYIFLSIAAHRIFQRDGANIFCRVPIPMTTAALGGTIEVPTIDGSKAKVTIPEGTQTGNQFRLRSKGMSVLRSPARGDMFIQAVVETPVNLTKRQKELLNEFNEAGEGEKAKNSPESQGFFAKVKELWEDLKEG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.209 kDa
Sequence
MAKDDYYELLGVQKGASEEELKKAYRKKAVQYHPDKNPGNKEAEEMFKKISHAYEVLKDPEKRAAYDRYGPAAFEGAGAGAGMGGMRGGGGFHDPFDIFREVFGQQGGMGGGIFEEMFGGGRGGGGQDGADLRYDLEITLEEAARGAEKEISFRKLVACERCDGSGAEPGSKRVTCPTCRGAGQVRRSGGIITFTQTCPTCGGMGTKIEKPCTVCHGEGRVRRTTKLNVRIPPGVDNGSRLRSSGNGEAGVAGGQNGDLYIVISVQEHELFERQGDDLFCEIPIKFTLATLGGTIEVPTLFGKASLKIPVGTQSGTTFRLRDKGMPSLRGGRQGDQLVRVHVEVPQSLTPEQRKILEDFARVSGDASEPTSRSFFEKAKKFF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.382 kDa
Sequence
MAKADYYETLGVSRTADEKELKSAFRKLAMQFHPDKNPDDNDAERKFKEINEAYETLKDPNKRAAYDRYGHAAFEHGGMGGGGFGGGGFGGGGGFSDIFEDIFGEMMGGGRGRARSSGGRERGADLRYNMEISLEEAFTGKTAQIRVPTSITCDVCSGSGAKPGTQPKTCGTCQGSGRVRAAQGFFSVERTCPTCHGRGQTIPDPCGKCHGQGRITEERSLSVNIPSGIEDGTRIRLQGEGEAGTRGGPSGDLYIFLSVKPHEFFQRDGADLYCAVPISMTTAALGGTFDVATLDGTKSRVTVPEGTQVGKQFRLKAKGMPVLRSSQVGDLYIQIQIETPQKLTKRQRELLQEFEQISSKDNNPESTGFFARMKDFFDTFSD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Anaplasma phagocytophilum (strain HZ)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.139 kDa
Sequence
MGSNDYYDLLGVSRGASEEEIKKSYRKKVFEYHPDRNPGNKEAEEKFKKISEAYDVLTDSDKRAAYDRYGHSAFANGMGGNQGFTGGFDGGFSTDFSDIFNDFFGGGFGKTSRQSSRENMRGSDLRYDIEVTLEDAFKGVKVPISYVTHVQCSHCSGSGGEGTAKSVKCGTCNGAGRIRTRKGFLTIEELCHTCSGEGEVVKNKCKRCAGSGRVRNEVGILVTVPRGIENGNKVRVNGKGEAGYRGARSGDLYVYVVVKDHKFFTRRGMDLYCNVPIKMTLAALGGEIEMPSIDGTWTKLKIPEGTQSNDKLRMRGKGMPDIQGGERRGDMYVQVTVETPVKLTKKQEELLKQFEDESNANSSPKFSGFFQKIKGIWKDISS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Geobacillus kaustophilus (strain HTA426)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.928 kDa
Sequence
MAKRDYYEILGVSKNATKDEIKKAYRKLSKQYHPDVNKAPDAAEKFKEIKEAYEVLSDDEKRARYDRFGHADPNETFGGGGFQGGGFDFGGFSGFGGFEDIFETFFGAGPRRRASGPRKGADVEYMMTLTFEEAAFGKETEIEIPREETCDTCQGSGAKPGTSPTSCPHCHGSGQVTSEQATPFGRIVNRRTCPVCGGTGRYIPEKCPTCGGTGRVKRRKKIHVKIPAGVDDGQQLRVAGQGEPGVNGGPPGDLYIIFRVEPHEFFKRDGDDIYCEVPLSFAQAALGDEIEVPTLHGHVKLKIPAGTQTGTRFRLKGKGVPNVRGYGQGDQHVIVRVVTPTKLTEKQKQLLREFERLGGDTMHDGPHGRFFEKVKKAFKGEA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.769 kDa
Sequence
MAKRDYYEVLGVSRTASADELKKAYRTKAKELHPDRNADNPQAEAQFKEVNEAYDVLRDADKKAAYDRYGHAAFEGGMGGGARAGGGYGQQGDFASAFSDVFEDLFGDFMGGRGGAPRSRAQRGSDLRYNLRVTLDEAYRGVQKTINVPASVACDACKGTGAEGGAEAVTCPTCSGMGKVRAQQGFFTVERTCPTCNGMGQIVKNPCKVCHGAGRVEKERSLSVNIPAGVETGTRIRLAGEGEAGMRGGPSGDLYIFIEVREHALFQRDGVHLFCRVPVSITAAALGGEVEVPTIDGGSSRVKIPAGSQTGKQMRLRGKGMPALRGGGAGDMLIELAVETPVNLTARQKELLREFEKLSEDNNPEGKSFFSKVKGFWDGMTG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.739 kDa
Sequence
MAKRDYYEVLGVSRTASADELKKAYRTKAKELHPDRNADNPQAEAQFKEVNEAYDVLRDADKKAAYDRYGHAAFEGGMGGGARAGGGYGQQGDFASAFSDVFEDLFGDFMGGRGGAPRSRAQRGSDLRYNLRVTLDEAYRGVQKTINVPASVACDACKGTGAEGGAEAVTCPTCSGMGKVRAQQGFFTVERTCPTCNGMGQIVKNPCKVCHGAGRVEKERSLSVNIPAGVETGTRIRLAGEGEAGMRGGPSGDLYIFIEVREHALFQRDGVHLFCRVPVSIAAAALGGEVEVPTIDGGSSRVKIPAGSQTGKQMRLRGKGMPALRGGGAGDMLIELAVETPVNLTARQKELLREFEKLSEDNNPEGKSFFSKVKGFWDGMTG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.757 kDa
Sequence
MAKRDYYEVLGVSRGASADELKKAYRTKAKELHPDRNADNPQAEAQFKEVNEAYDVLRDADKKAAYDRYGHAAFEGGMGGGGGARGAYGQQADFASAFSDVFEDLFGDFMGGRGGAARSRAQRGSDLRYNLRVTLDEAYRGVQKTINVPASVACDSCKGTGAEGGAEPVTCPTCSGMGKVRAQQGFFTVERTCPTCNGMGQIVKNPCKSCHGAGRVEKERTLSVNIPAGVETGTRIRLAGEGEAGMRGGPSGDLYIFIEVREHALFQRDGVHLFCRVPVSITAAALGGEVEVPTIDGGSSRVKIPAGSQTGKQMRLRGKGMPALRGGGAGDMLIELAVETPVNLTARQKELLREFEKLSEDNNPEGKSFFSKVKGFWDGMTG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus brevis (strain ATCC 367 / JCM 1170)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.836 kDa
Sequence
MAQSDLYGVLGVAKDASQDEIKKAYRKLSKKYHPDLNKAPDAAEKFKEVQDAYDVLGDEQKRANYDQSGSADGAQGGFGGFGGGQQGGFGGFGGGGGFDDIFNQFFGGGGGQRNPNAPRPGRDLQYQMDLTFEEAIFGKKTKIKYNREAQCHTCGGNGAKPGTSPVTCHQCGGSGYVTTETNTPLGRMRSQQPCPVCHGTGQEIKEKCPTCGGSGHEEERHEVEVTIPAGVDDGQQMRLQGQGEAGQNGGGYGDLFIIFKVQPSKDFRRDGTEIYFDQDISFVQATLGDDVTVKTVHGDVKLKVPAGTQGGTTFRLRGKGAPRLRGNGNGDEHVTIKVVTPKNLNKGQRDALRDFAKASGESVTGSGKGNLFNKMRDKFNEN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chlorobium luteolum (strain DSM 273 / 2530)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.881 kDa
Sequence
MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKDAEDHFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASGGGGGQYGGGADFSDIFSAFNDMFGGGGGGSQRRRAASGIPGVDLKIRLKLTLEEIAKGVEKTIKIKKQVPCKECNGSGSKTGATETCPTCHGAGEVRQASKTMFGQFVNIAACPTCGGEGRIVKDRCPSCYGEGIKQGEVTVKVNVPAGVQEGNYLTLRGQGNSGPRGGAPGDLIVMIEEKPHELFVRNGDDVIYSLAVSFPDLVLGTKVDVPTLEGAVKLTIPAGTQPETMLRIPGHGIGHLRGSGKGDQYVRVNVYVPKELTQQDKDLLRDLRKSPSIAPEAHSAGGAKSFFEKARDIFG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haemophilus influenzae (strain PittGG)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.243 kDa
Sequence
MAKKDYYEVLGLKKGASENDIKRAYKRLASKHHPDKNQGSKEAEEKFKEINEAYEVLGDDQKRAAYDQYGHAAFEQGGGAGGFGGGFGGADFGDMFGDIFGDIFGGGGRGRQRVVRGEDLRYDLEITLEEAVKGTTKDIQINTLAHCDSCGGSGAEKGSKVETCPHCHGSGRIRRQQGFFVSESICPSCHGSGKKIEKPCRSCHGEGRVHKKENLSVKIPAGVDTGNQLRLAGKGAVGENGAPAGDLYVVIHVREHHIFERDGSNLYCEVPISFAIAALGGEIEVPTLDGRVKLKIPAETQTGKLFRMRGKGVASTRSGYAGDLICRIVVETPVNLTSEQKELLHKLEESLQGKDLSKHAPKSSGFLDGVKKFFDNLGKSDK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.222 kDa
Sequence
MAKKDYYEVLGLQKGASEDEIKRAYKRLASKHHPDKNQGSKEAEEKFKEINEAYEVLGDDQKRAAYDQYGHAAFEQGGGAGGFGGGFGGADFGDMFGDIFGDIFGGGGRGRQRVVRGEDLRYDLEISLEEAVKGTTKDIQINTLAHCDSCGGSGAEKGSKVETCPHCHGSGRIRRQQGFFVSESICPTCHGSGKKIEKPCRNCHGEGRVHKKENLSVKIPAGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVREHNIFERDGSNLYCEVPISFATAALGGEIEVPTLDGRVKLKIPAETQTGKLFRMRGKGVASTRSGYAGDLICRIVVETPVNLTSEQKELLHKLEESLQGKDLSKHAPKSSGFLDGVKKFFDNLGKSDK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Length
382 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.203 kDa
Sequence
MATKRDYYEILGLPKDASVEDIKKTYRKLALQYHPDRNKDPGAEDKFKEISEAYAVLSDTEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYITFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPTCGGTGQVRTTRSTLGMQFISTTTCSTCHGRGQIIESPCPVCGGAGRVRNKRTITVNVPAGADSGMSLRLSGEGDSGEPGAPSGDLYIIIHVMEHRHFKRVDYDVISELSITFTQAALGADVMVDTLYGKVKMNIPAGTQTHSVFRLRDKGIQRLHGHGKGDQLVRVIIKTPTKLNQEQKELLRQFENLSKGKKPQEEEKSKAEKHKKGIFEKVKDAFES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.854 kDa
Sequence
MAKRDYYEVLGCDRGADETVLKASFRKLAMKWHPDKNPGDPEAEIRFKEISEAYEVLKDPQKRGAYDRYGHAAFENGGGPGGAGFNADFASTFADIFDDLFGGSMGRSGARSAGGRARGADLRYNMDITLEEAFSGKTAQISIPTSISCEVCSGSGAKAGTQPKTCRTCNGAGKIRHAQGFFTLERTCPSCQGRGTVIEDPCPNCGGAGRVTRERTLQVQIPAGVEDGTRIRLGGEGEAGVRGGPPGDLYIFLSIEPHTFFQREGADLYCRAPISMVTAALGGTVEVPTIGGEKTKVKIPEGTQSGKRLRLPGAGMPVLRSRSFGDMYVQVVVETPQNLTKRQKELLAEFEGLSSTDTHPESNGFFAKMKDFFQGASSDND

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.709 kDa
Sequence
MADKRDYYEVLGISKSASDDEIKKAYRKLAKQYHPDANPGDQTAEAKFKEASEAYAVLSDPEKKRQFDQFGHAAFEQGGGGAGGFDFNMGDMGDIFGDIFGDIFGGGRRSRASNGPMNGANLRTAIRITFEEAVFGCEKELELSLKDECETCHGSGAKPGSSAETCHKCNGKGQVTFTQQSLFGMVRNVQTCPDCRGTGKIIKEKCPDCYGSGYISRKKKIQVSVPAGIDNGQSIRIRGKGEPGTNGGERGDLLVEVNVSRHPIFQRQDYDIYSTAPMTFTQAALGGDVRISTVDGDVLYEVKPGTQTDTKVRLRGKGVPTLRNKDVRGDHYVTLVVQVPTKLNNEQKDLLKKFEESVSGKKSEDTTTEDTKEKKKKFFGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.349 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKYHPDRNPEGKDGKIAEEKFKEVKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGAQGYGGFAEAFGDIFGDIFGQQAGGRRGGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFTMQQTCPKCHGSGKYIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKAHPMFERDGDDLHCQMPISFATAALGGDLEVPTLSGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKEMLRQFDRSVHEGGSRHSPQEQSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.822 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKYHPDRNSGDAGAAEKFKEVKEAYEILTDAQKKAAYDQYGHAAFEQGAGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGPRAQRGSDLRYNMELSLEEAVRGCSKEIEVPTLVHCDACDGSGAKKGTSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPAETQTGRMFRMRGKGVKGVRSAALGDLIVKLVVETPVNLSARQKELLKEFEESCGGEAATKHKPKAEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.093 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGQQRAQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCDGSGAKKGSSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNECHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPTETQTGRMFRMRGKGVKGVRGGGVGDLIVKLVVETPVNLSSRQKELLKEFDESCGGDAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.822 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKYHPDRNSGDAGAAEKFKEVKEAYEILTDAQKKAAYDQYGHAAFEQGAGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGPRAQRGSDLRYNMELSLEEAVRGCSKEIEVPTLVHCDACDGSGAKKGTSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPAETQTGRMFRMRGKGVKGVRSAALGDLIVKLVVETPVNLSARQKELLKEFEESCGGEAATKHKPKAEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio cholerae serotype O1 (strain M66-2)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.822 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKYHPDRNSGDAGAAEKFKEVKEAYEILTDAQKKAAYDQYGHAAFEQGAGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGPRAQRGSDLRYNMELSLEEAVRGCSKEIEVPTLVHCDACDGSGAKKGTSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPAETQTGRMFRMRGKGVKGVRSAALGDLIVKLVVETPVNLSARQKELLKEFEESCGGEAATKHKPKAEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.026 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEVLTDSQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGGHRAQRGADLRYNMELTLEEAVRGVTKEIEVPTLVHCDSCDGSGAKKGSSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNECHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPSGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPSETQTGRMFRMRGKGVKGVRGGGIGDLIVKLVVETPVNLSSRQKELLKEFEESCGGEAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio tasmaniensis (strain LGP32)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.051 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDDSAADKFKEVKVAYEILTDAQKKAAYDQYGHAAFEQGGMGGGGYGGGGQGDFGDIFGDVFGDIFGGGRRGGGQARAQRGSDLRYNMELSLEEAVRGVSKEIEVPTLVECDICDGSGAKAGSSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCNGKGKIIKDPCNSCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVHVKEHNIFERDGNNLYCEVPVSFSMAALGGEVEVPTLDGRVNLKVPEETQTGRMFRMRGKGVKGVRGGGVGDLIVKLVVETPVKLSSRQKELLREFEETCCGEAASKHKPKSEGFFSGVKNFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio vulnificus (strain CMCP6)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.226 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGHARPQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCEGTGAKKGTSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGERGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPSETQTGRMFRMRGKGVKGVRGGAIGDLIVKLVVETPVNLSSRQKELLKEFEESCCGEAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio vulnificus (strain YJ016)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.226 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGHARPQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCEGTGAKKGTSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGERGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPSETQTGRMFRMRGKGVKGVRGGAIGDLIVKLVVETPVNLSSRQKELLKEFEESCCGEAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.349 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKYHPDRNPEGKDGKIAEEKFKEVKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGAQGYGGFAEAFGDIFGDIFGQQAGGRRGGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFTMQQTCPKCHGSGKYIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKAHPMFERDGDDLHCQMPISFATAALGGDLEVPTLSGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKEMLRQFDRSVHEGGSRHSPQEQSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.822 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKYHPDRNSGDAGAAEKFKEVKEAYEILTDAQKKAAYDQYGHAAFEQGAGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGPRAQRGSDLRYNMELSLEEAVRGCSKEIEVPTLVHCDACDGSGAKKGTSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPAETQTGRMFRMRGKGVKGVRSAALGDLIVKLVVETPVNLSARQKELLKEFEESCGGEAATKHKPKAEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.093 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGQQRAQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCDGSGAKKGSSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNECHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPTETQTGRMFRMRGKGVKGVRGGGVGDLIVKLVVETPVNLSSRQKELLKEFDESCGGDAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.822 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKYHPDRNSGDAGAAEKFKEVKEAYEILTDAQKKAAYDQYGHAAFEQGAGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGPRAQRGSDLRYNMELSLEEAVRGCSKEIEVPTLVHCDACDGSGAKKGTSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPAETQTGRMFRMRGKGVKGVRSAALGDLIVKLVVETPVNLSARQKELLKEFEESCGGEAATKHKPKAEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio cholerae serotype O1 (strain M66-2)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.822 kDa
Sequence
MSKRDFYEVLGVGRDASERDIKKAYKRLAMKYHPDRNSGDAGAAEKFKEVKEAYEILTDAQKKAAYDQYGHAAFEQGAGGFGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGPRAQRGSDLRYNMELSLEEAVRGCSKEIEVPTLVHCDACDGSGAKKGTSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPAGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPAETQTGRMFRMRGKGVKGVRSAALGDLIVKLVVETPVNLSARQKELLKEFEESCGGEAATKHKPKAEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.026 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEVLTDSQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGGHRAQRGADLRYNMELTLEEAVRGVTKEIEVPTLVHCDSCDGSGAKKGSSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNECHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEMGAPSGDLYVQVHVKEHHIFERDGNNLYCEVPVSFAMAALGGEVEVPTLDGRVSLKVPSETQTGRMFRMRGKGVKGVRGGGIGDLIVKLVVETPVNLSSRQKELLKEFEESCGGEAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio tasmaniensis (strain LGP32)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.051 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDDSAADKFKEVKVAYEILTDAQKKAAYDQYGHAAFEQGGMGGGGYGGGGQGDFGDIFGDVFGDIFGGGRRGGGQARAQRGSDLRYNMELSLEEAVRGVSKEIEVPTLVECDICDGSGAKAGSSAQTCGTCHGHGQVQMRQGFFAVQQTCPTCNGKGKIIKDPCNSCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVHVKEHNIFERDGNNLYCEVPVSFSMAALGGEVEVPTLDGRVNLKVPEETQTGRMFRMRGKGVKGVRGGGVGDLIVKLVVETPVKLSSRQKELLREFEETCCGEAASKHKPKSEGFFSGVKNFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio vulnificus (strain CMCP6)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.226 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGHARPQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCEGTGAKKGTSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGERGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPSETQTGRMFRMRGKGVKGVRGGAIGDLIVKLVVETPVNLSSRQKELLKEFEESCCGEAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vibrio vulnificus (strain YJ016)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.226 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDESAADKFKEVKEAYEILTDPQKKAAYDQYGHAAFEQGGGGFGGGFGGGGADFGDIFGDVFGDIFGGGRRGGGHARPQRGADLRYNMELSLEEAVRGVSKEIEVPTLVHCDTCEGTGAKKGTSAETCGTCHGHGQVQMRQGFFAVQQTCPTCHGKGKIIKDPCNVCHGQGRKQKTKTLNVKIPAGVDTGDRIRLSGEGEAGERGAPAGDLYVQVHVREHHIFEREGNNLYCEVPVSFAMAALGGEVEVPTLDGRVNLKVPSETQTGRMFRMRGKGVKGVRGGAIGDLIVKLVVETPVNLSSRQKELLKEFEESCCGEAATKHKPKSEGFFNGVKKFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.44 kDa
Sequence
MSKRDYYEVLGIERGADQKEIKKAYRRLAQKYHPDRNPDDDTAAEKFREVSEAYEVLTDEEKRSAYDQFGHAGVDGQAGGGFGGGGFGGGAGGFSDIFGDVFGDIFGGGGRRNPNAPQRGSDLRYNLELDLEDAVAGTTVDIRVPRHIECEHCDGDGAEPGSTKETCPTCHGQGQVRMQQGFFAVQQTCPTCHGAGQTIKVPCRKCHGEGRVRETRTLSVKIPAGVDTGDRIRLNNEGEAGLNGGPPGDLYVQAAIKPHPIFERDGRHLQCEVPINFIDATLGGELEVPTLDGRVKLKIPPETQTGKMFRLKGKGVKPVRGGPPGDLLCKVVLETPVNLSDEQKDLLRQFQDSLDGSNSHHSPKKTSFFDGVKKFFEDMKP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Geobacillus thermodenitrificans (strain NG80-2)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.758 kDa
Sequence
MAKRDYYEVLGVSKNATKDEIKKAYRKLSKQYHPDINKAPDAAEKFKEIKEAYEVLSDDEKRARYDRFGHADPNEAFGGGFQGGGFDFGGFSGFGGFEDIFETFFGGGSRRRASGPRKGADLEYMMTLTFEEAAFGKETEIEVPHEETCDTCHGSGAKPGTSPQSCPHCHGSGQVTSEQATPFGRIVNRRTCPVCGGTGRHIPEKCPTCGGTGHVKKRKKIHVKIPAGVDDGQQLRVAGKGEPGVNGGPPGDLYIIFRVQPHEFFKRDGDDIYCEVPLSFAQAALGDEIEVPTLHGDVKLKIPAGTQTGTRFRLKGKGVPNVRGYGQGDQHVIVRVVTPTKLTEKQKQLLREFDRLGGETMHDGSHGRFFEKVKKAFKGET

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haemophilus influenzae (strain 86-028NP)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.154 kDa
Sequence
MAKKDYYEVLGLQKGASEDDIKRAYKRLASKHHPDKNQGSKEAEEKFKEINEAYEVLGDDQKRAAYDQYGHAAFEQGGGTGGFGGGFGGADFGDMFGDIFGDIFGGGRGRQRVVRGEDLRYDLEISLEEAVKGTTKDIQINTLAHCDSCGGSGAEKGSKVETCPHCHGSGRIRRQQGFFVSESICPTCHGSGKKIEKPCRSCHGEGRVHKKENLSVKIPAGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVREHNIFERDGSNLYCEVPISFATAALGGEIEVPTLDGRVKLKIPAETQTGKLFRMRGKGVASTRSGYAGDLICRIVVETPVNLTSEQKELLHKLEESLQGKDLSKHAPKSSGFLDGVKKFFDNLGKSDK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodobacter sphaeroides (strain KD131 / KCTC 12085)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.682 kDa
Sequence
MAKRDYYEVLGVSRTASADELKKAYRTKAKELHPDRNADNPQAEAQFKEVNEAYDVLRDADKKAAYDRYGHAAFEGGMGGGARAGGYGQQGDFASAFSDVFEDLFGDFMGGRGGAPRSRAQRGSDLRYNLRVTLDEAYRGVQKTINVPASVACDACKGTGAEGGAEAVTCPTCSGMGKVRAQQGFFTVERTCPTCNGMGQIVKNPCKVCHGAGRVEKERSLSVNIPAGVETGTRIRLAGEGEAGMRGGPSGDLYIFIEVREHALFQRDGVHLFCRVPVSIAAAALGGEVEVPTIDGGSSRVKIPAGSQTGKQMRLRGKGMPALRGGGAGDMLIELAVETPVNLTARQKELLREFEKLSEDNNPEGKSFFSKVKGFWDGMTG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.801 kDa
Sequence
MKRDYYEILGVARNATPEEIKKAYRKLARKYHPDVNKDDPNAAEKFKEINEAYEVLSDPEKRARYDQFGHAGVDGNFAGQGGFGGGAGINFEDIFSGFGGFGDLFDMVFGSGRKARQGPVPGDDIEAVLELTLEEAVFGGEKELRVTRTETCGHCHGNGAEPGTPIITCPTCQGRGQIHQEVKTLFGRMVRSQVCSTCRGEGKIPKTPCRECGGSGLVRKTRSITVKIPPGIDHGHRLRIAGGGEAGRFGGPPGDLYVYIKIKPHKLFKREDIHLKLEKEISFVQAALGAKVEIPTIDGGTEILEIPEGTQTGTVFTIKGKGVPVVNGSGRGNLYVTVKVVTPTKLTERQKQLLREFEEISKQKEETFKEKFNKFKNKFAL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.249 kDa
Sequence
MKVDYYEILGVTRECDDKKLKSAFRKLAMQYHPDRNAGDKEAERKFKEIGEAYEVLKDPQKRAAYDRFGHAAFENNNNGGGSPFSGFSAGGFADIFEDFFGEIMGGGHRKRSDGRERGADLSYNMEVTLEEAFSGKTAQINIPSSVVCDACEGSGAKKGSKPQTCGTCHGAGRVRAAQGFFSIERTCPVCHGRGETIKDPCPKCQGTRRVEKNRSLSVNIPAGIEDSTRIRLSGEGDAGIRGGPSGDLYIFLSVKPHEFFQREGADLHCRVPISMVTAALGGEFEVSDLDGIKARVKIPEGTQNGRQFRLKGKGMPMLRRQQVRGDLYIHITIETPQKLTQEQRELLQKFEKLSNHENSPQSHGFFSRMKEFFENISGKNE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bifidobacterium longum (strain NCC 2705)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.593 kDa
Sequence
MADYYETLGVERGASDDEIKKAYRKLSRKYHPDIAGPEFEDKFKEVNNAYDVLSNPDKRRMYDSGVDPNNPNAGAGGFSGAGFGDMSDVFSTFFGSAFGGGSQGPVPRTQPGRDALASASIDLKTAVFGGTAHVKINTFSLCQECGGSGAQGGAQPVTCPDCHGQGFMQKVVRTMLGQMMTSAPCERCEGHGTIIQNPCPSCMGHGRVRTTRTVGVTVPAGINDNARLRLANQGEVGEGGGAAGDLYIDIRIKADKQFTRDGDDLHCWIQVPMSWAVLGHDLSIDTFDGEKTVSIPAGCQTEDTVTLKGLGVTNIRNKDERGNLIAHVNVLIPTKLNETERGLIEQFAASHDSGATHVSQASRPQAGQKKGFFSKLKDALS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Length
381 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.662 kDa
Sequence
MSKRDYYDVLGVSKGASADEIKKAYRGKAKELHPDRNKDNPDAESLFKEVNEAYEVLKDAEKKAAYDRFGHAAFEGGMGGGQRPGGGFGSGDFSSAFSDVFEDLFGDFMGGQRGGGGRRAARGSDLRYNLRVTLEEAFSGLQKTINVPTAVACSSCEGTGAEGGVEPTTCPTCSGMGKVRAQQGFFTVERTCPTCSGLGQIIKNPCKSCRGQGRVEKDRALSVNIPAGVETGTRIRLAGEGEAGMRGGPPGDLYIFVEVAKHELFERDGVNLYCRVPVSMAKAALGGAIEVPTIDGGRGRVQVPAGSQSGRQMRLRSKGMPALRGGGIGDMFIELAVETPVNLTSKQKDLLREFDELSEDNNPETKSFFSSVKSFWDGMKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.55 kDa
Sequence
MAEQDLYKVLGVEKDASQDEIKKAYRKLSKKYHPDLNHEPGAEEKFKAVNEAYETLGDAQKRAQYDQFGSTGGQQGFGGAGGFGGQDFGGFGGGGGFEDIFSSFFGGGAGGSRRSNPTAPQQGRDLQYEMTLKFEDAIFGKKTTITYNREEQCETCGGSGAKPGTSPVTCSKCHGAGYIQVQTNTPLGRMMSQQVCDVCHGTGKEIKDKCATCGGSGHTEQSHSIKVTVPAGVEEGQQMRLQNQGEAGTNGGPYGDLFIIFRVEPSKDFERDGATIYFKLPIDFVQAALGDEVQVKTVHGDVKLKIPAGTQTGTTFRLRGKGAPRLRGNGNGDERVTVNIETPTHLNKGQKEALKTFAKASGKSVAGNGKSSLFDKLRGV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Laribacter hongkongensis (strain HLHK9)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.751 kDa
Sequence
MSKKDFYDVLGVNRDASDDDIKKAYRKLAMKYHPDRNPDSKDAEEKFKEAKEAYEILSDAQKRAAYDQYGHAGVDPQAGFGGAGGQQGFGGFGDAFADIFGDIFGGGARAGGGGGRNAVYRGSDLRYNLEITLEEAARGCEKQIRIPTMEECSHCHGSGAKPGTEPKTCPTCGGAGQVRMQQGFFSIQQTCPTCHGSGKQITDPCNICHGAGRVKSQKTLNVKIPAGVDDGDRIRLSGEGEPGTNGGPAGDLYVVTHIKPHAVFERDGMDLHCEMPISFATAALGGEIEIPTLDGAAKLRIPAETQSGQVFRLRGKGIKALRASQHGDLMCHVQVETPVKLTDRQKELLREFDAISQGAPAKHNPKAQSFMDKLKDFFGG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Delftia acidovorans (strain DSM 14801 / SPH-1)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.995 kDa
Sequence
MSKRDFYEVLGVAKNASDDDIKKAYRKLAMKYHPDRNQGDAAREAEEKFKEAKEAYEMLSDSNKRAAYDQYGHAGVDPNRGMGGGAEGFGGFAEAFGDIFGDMFNQGGGRRGGAGGGRQVYRGNDLSYAMEITLEEAAHGKDAQIRIPSWDGCDTCHGSGAKPGTSAKTCTTCNGMGSVQMRQGFFSVQQTCPHCRGTGKIIPEPCTSCGGQGKVKRQKTLEVKIPAGIDDGMRIRSSGNGEPGTNGGPAGDLYIEIRIKDHDIFERDGDDLHCNVPVSFITAALGGEIEVPTLSGKAAIDIPEGTQAGKQFRLRGKGIKGVRSSYPGDLYCHIVVETPVKLTEYQRKLLRELEESLKKGGAKHSPSGESWTDRLKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.47 kDa
Sequence
MAKRDYYEVLGVERGSSEADLKKAYRRLAMKHHPDRNPDDKASEELFKEANEAYEVLSDASKRAAYDQYGHAGVDPSMGGGGGFGGGAGGANFSDIFGDVFSDFFGGGRGGGGGGRGGAQRGSDLRYTLELNLEEAVRGTNVNIRVPTLVNCKPCDGSGAKKGSSPVTCPTCGGIGQVRMQQGFFSVQQTCPRCHGHGKIISDPCDSCHGEGRVEESKTLSVKVPPGVDTGDRIRLSGEGEAGTQGGPTGDLYVVINVREHAIFQRDGKHLFCEVPISFTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLMCHVAVETPVNLSKRQRELLEEFRTSLENDESHSPKASGWFEGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.459 kDa
Sequence
MSKRDYYEVLGVSKDASERDIKKAYKRLAMKYHPDRTSGDKELETKFKEVKEAYEILTDAQKRQTYDQYGHAAFEQGGGGGGHGGFGGGHGDFGDVFGDVFGDIFGGGGGRRQSRQQRGSDLRYNMDLSLEEAVRGKEVEIKIPTWVGCDPCDGSGAKAGSKPKTCTTCHGAGQVQMRQGFFAVQQTCPTCQGQGQIISNPCDSCHGQGRVEKTKTLSVKIPAGVDTGDRIRLTGEGEAGMHGAPSGDLYVQVSVREHRIFVRDANNLHCEVPISFTTAGLGGEIEVPTLDGRAKLKIPSETQTGKMFRMRGKGVKSVRSGAIGDLICKVVIETPINLNERQRELLEELEESMGKDSSKNRPKEQGFFDGVKKFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Delftia acidovorans (strain DSM 14801 / SPH-1)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.995 kDa
Sequence
MSKRDFYEVLGVAKNASDDDIKKAYRKLAMKYHPDRNQGDAAREAEEKFKEAKEAYEMLSDSNKRAAYDQYGHAGVDPNRGMGGGAEGFGGFAEAFGDIFGDMFNQGGGRRGGAGGGRQVYRGNDLSYAMEITLEEAAHGKDAQIRIPSWDGCDTCHGSGAKPGTSAKTCTTCNGMGSVQMRQGFFSVQQTCPHCRGTGKIIPEPCTSCGGQGKVKRQKTLEVKIPAGIDDGMRIRSSGNGEPGTNGGPAGDLYIEIRIKDHDIFERDGDDLHCNVPVSFITAALGGEIEVPTLSGKAAIDIPEGTQAGKQFRLRGKGIKGVRSSYPGDLYCHIVVETPVKLTEYQRKLLRELEESLKKGGAKHSPSGESWTDRLKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.47 kDa
Sequence
MAKRDYYEVLGVERGSSEADLKKAYRRLAMKHHPDRNPDDKASEELFKEANEAYEVLSDASKRAAYDQYGHAGVDPSMGGGGGFGGGAGGANFSDIFGDVFSDFFGGGRGGGGGGRGGAQRGSDLRYTLELNLEEAVRGTNVNIRVPTLVNCKPCDGSGAKKGSSPVTCPTCGGIGQVRMQQGFFSVQQTCPRCHGHGKIISDPCDSCHGEGRVEESKTLSVKVPPGVDTGDRIRLSGEGEAGTQGGPTGDLYVVINVREHAIFQRDGKHLFCEVPISFTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLMCHVAVETPVNLSKRQRELLEEFRTSLENDESHSPKASGWFEGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.459 kDa
Sequence
MSKRDYYEVLGVSKDASERDIKKAYKRLAMKYHPDRTSGDKELETKFKEVKEAYEILTDAQKRQTYDQYGHAAFEQGGGGGGHGGFGGGHGDFGDVFGDVFGDIFGGGGGRRQSRQQRGSDLRYNMDLSLEEAVRGKEVEIKIPTWVGCDPCDGSGAKAGSKPKTCTTCHGAGQVQMRQGFFAVQQTCPTCQGQGQIISNPCDSCHGQGRVEKTKTLSVKIPAGVDTGDRIRLTGEGEAGMHGAPSGDLYVQVSVREHRIFVRDANNLHCEVPISFTTAGLGGEIEVPTLDGRAKLKIPSETQTGKMFRMRGKGVKSVRSGAIGDLICKVVIETPINLNERQRELLEELEESMGKDSSKNRPKEQGFFDGVKKFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Paraburkholderia xenovorans (strain LB400)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.757 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKHHPDRNPGNKDAEGHFKEVKEAYEMLSDSQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGGGRAGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCSGSGSVRMSQGFFSIQQTCPKCHGTGTYIPDPCGHCHGAGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKQHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTEPQRDLLKQFEKALVEGGSRHSPQSKSWFDRVKSFFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Photobacterium profundum (strain SS9)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.802 kDa
Sequence
MSKRDFYEVLGVGRDAGERDIKKAYKRLAMKFHPDRNQEADATEKFKEVKTAYEILTDPQKKAAYDQYGHAAFEQGSGGGGYGGGGGADFGDIFGDVFGDIFGGAGGGRRQQQRAQRGSDLRYNMELTLEEAVRGCSKEIRVPTLVGCDSCDGSGAKRGSSATTCGTCHGQGQVQMRQGFFAVQQACPHCHGRGKIIKDPCNSCHGQGRVEKTKTLSVKIPAGVDTGDRIRLSGEGEAGEFGAPAGDLYVQVHVAEHSIFERDGNNLYCEVPVSFTMAAVGGEVEVPTLNGRVNLKVPSETQTGRMFRMRGKGVKSVRGGAVGDLICKLVVETPVNLSSHQKELLKELEESFGGKAAGKHKPKSEGFFNGVKKFFDDLTG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Polaromonas naphthalenivorans (strain CJ2)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.681 kDa
Sequence
MAKKDYYDTLGVPKNASDEDIKKAYRKLAMKHHPDRNQGDTSKVSEDKFKEAKEAYEMLSDAQKRAAYDQYGHAGVDPNRGGGPGAEGFGGFAEAFGDIFGDVFGGQRGGAQGGGGRQVYRGGDLSYAMEVTLEEAAAGKEAQIRIPSWDDCGICHGTGAKPGTKVATCTTCHGHGVVQMRQGFFSVQQTCPQCKGSGKLIPSPCVACHGVGKTKNNKTLEVKIPAGIDDGMRIRSTGNGEPGTNGGPPGDLYIEIRLKKHDIFERDGDDLHCSMPISFMTAALGGEIEVPTLAGKAAIDIPEGTQAGKQFRLRGKGIKGVRSSYPGDLYCHITVETPVKLTEHQRKLLKELDESIKKGGAKHSPSEEGWTDKLKNFFGA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.156 kDa
Sequence
MAKKDYYDTLGVPKNASDDDIKKAYRKLAMKHHPDRNQGDKSKVSEEKFKEAKEAYEVLSDENKRMAYDQYGHAGVDPNMRGGGPGAEGFGGFAEAFGDIFGDVFGGQRGGQQRGGRQVYRGGDLSYAMEITLEEAAHGKEAQIRIPSWDDCNTCHGSGAKPGTKVVTCTTCHGHGVVQMRQGFFSVQQTCPQCKGTGKLIPEPCVACHGVGKTKNNKTLEVKIPAGIDDGMRIRSTGNGEPGTNGGPPGDLYIEIRIKKHEIFERDGDDLHCAVPISFTTAALGGEIEVPTLAGKAAIDIPEGTQAAKQFRLRGKGIKGVRSSYPGDLYCHITVETPVKLTEHQRKLLKELDESLKKGGARHSPSEEGWADKLKSFFSA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / NBRC 14720 / NCIMB 2260 / Gabara)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.816 kDa
Sequence
MSEDFYSVLGVSRDADEDEIKQAYRKKASEYHPDVSDDPNAEEKFKQVKKAKEVLLDDEKRRMYDQMGHERFQEAEKRGATDTDRGRGGMGGMGGGGMGGMNDIFEQFFGGGGRSQSRSGPRQGSDLKTRLKVDLEDAYHGVTKQLTVTRPEECPDCDGAGHPPDADSRTCSACDGRGQQTTVRQTALGRVQQTRECPQCDGKGTIYSETCSTCRGDGQVRNETTLQVEVPAGIRDGQTLRMDGEGAPGENGGRKGDLLVEIRIDDHETFERDGDDLRCRHPISFPQAVFGDTVEVPTLDGAVEMDVPAGTQSGETFRLRGKGMPRLKRRGHGDLYVQVRVVTPESLNEEQREALEAFAEAGGEEIDVEQGFFEKLKSSF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.926 kDa
Sequence
MAKRDYYEALGVARNASDAEIKKAYRRLAMRYHPDRNPDDKAAEEHFKEIQEAYDVLSDARKRTAYDQFGHAGVGAGASAGPGGHGFEGGSNFGDIFGDVFNDIFGAAAGRGGRRQAYRGADLRYNLDLTLEEAVAGTTAKIRIPTYVACKACEGSGAKPGTSPITCPTCGGHGQVRMQQGFFSLQQTCPRCHGSGQIVDSPCSTCRGEGRVREHKTLSVKIPPGVDTGDRIRLTGEGEAGESGGPPGDLYVQVQIKAHSIFSREGDALHCEVPVSFVAAALGGELDVPTLTGRAKLKIPAGTQSGQVFRLRGKGVSPVRGGSAGDLLCRVMVETPVNLNQEQKELLEKFEASMNRNKKHSPKHHSWLEGVKRFFEDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.817 kDa
Sequence
MAKKDYYEVLGLQKGASENDIKRAYKRLASKHHPDKNQGSKDAEEKFKEINEAYEVLGDAEKRAAYDQYGHAAFEQGGGAGGFGGGFGGGGFGGFEDIFSEMFGGGFGGGGRRNHVVRGDDLRYDIEISLEEAVKGCKKDIRISTLAECDTCHGSGAEKGSKVETCSHCHGSGRIRRQQGFFVTEAVCPSCHGSGKKIEKPCKSCHGDGRVQKAKNLSVTIPAGVDTGNQLRLSGEGAAGENGAPAGDLYVVIHVREHDIFERDGSNLYCEVPISFTMAALGGEIEVPTLDGKLKLKIPAETQTGKLFRVRGKGVASPRGGYAGDLICKVVVETPVALNDEQKDLLRKLEESLAGKSKHRPQQESFLDSVKNFFSNLGKH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.91 kDa
Sequence
MAKKDYYEVLGLQKGASENDIKRAYKRLASKHHPDKNQGSKDAEEKFKEINEAYEVLGDAEKRAAYDQYGHAAFEQGGGAGGFGGGFGGGGFGGFEDIFSEMFGGGFGSGGRRQRVVRGDDLRYDIEISLEEAVKGCKKDIRISTLAECDTCHGSGAEKGSKVETCSHCHGSGRIRRQQGFFVTEAVCPSCHGSGKKIEKPCKSCHGDGRVQKAKNLSVTIPAGVDTGNQLRLSGEGAAGENGAPAGDLYVVIHVREHDIFERDGSNLYCEVPISFTMAALGGEIEVPTLDGKLKLKIPAETQTGKLFRVRGKGVTSPRGGYAGDLICKVVVETPVALNDEQKDLLRKLEESLASKSKHRPQQEGFLDSVKNFFSNLGKH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.142 kDa
Sequence
MSKRDFYEVLGVSKDADEREIKKAYKRLAMKYHPDRNQGDAGAEEKFKEVKEAYEILTDANLRARYDQYGHAGVDQSQGGGGHGGFGGGADFGDIFGDVFGDIFGGSRGGGRRGPARGSDLRYTMELTLEEAVRGVSKEIKVPTLVHCEVCNGSGAHTGSSAQTCPTCHGSGQVQMRQGFFAVQQACPHCHGRGKIIKDPCRKCHGEGRYQKTKTLSVKIPAGVDTGDRIRLSGEGEAGEAGAPAGDLYVQVHVKEHEIFVRDGNNLYCEVPISFTAAALGGEIEVPTLDGRVKLKVTPETQTGKMFRMRGKGVKSVRSGQVGDLMCKVVVETPVKLTESQKELLRQLDESFSGAAAKTHKPKSEGFFEGVKRFFDDLTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Aeromonas salmonicida (strain A449)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.191 kDa
Sequence
MSKRDFYEVLGVSKGADEREIKKAYKPLAMKFHPDRNQGDAASEEKFKEVKEAYEILTDENLRARYDQYGHAGVDQSQGGGGHGGFGGGADFGDAFGDIFGDIFGGRNGGGRRGPARGSDLRYTMELTLEEAVRGVSKEIKVPSLVHCEVCNGSGAHTGSTAQTCPTCHGAGQVQMRQGFFAVQQACPHCHGRGKIIKDPCRKCHGEGRYQKTKTLSVKIPAGVDTGDRIRLSGEGEAGEAGAPAGDLYVQVHVKEHEIFVRDGNNLYCEVPISFTAAALGGEIEVPTLDGRVKLKVTPETQTGKMFRMRGKGVKSVRSGQVGDLMCKVVIETPVKLTESQKELLRQLDESFSGAAAKTHKPRSEGFFEGVKRFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Agrobacterium vitis (strain S4 / ATCC BAA-846)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.054 kDa
Sequence
MAKADFYETLGVSKTADEKELKSAFRKLAMKFHPDKNPGDAESERKFKEINEAYETLKDPQKRAAYDRFGHAAFEQGGMGSAGGGGGFAGGGFSDIFEDIFGEMMGGGRGGNARGRSTGGRERGADLRYNMEISLEEAFTGKTAQIRVPTSITCEVCSGSGAKPGTKPTTCATCQGSGRVRAAQGFFSIERTCPTCQGRGQTISDPCGKCHGQGRVTEERQLSVSIPSGIEDGTRIRLQGEGEAGLRGGPSGDLYIFLSVKPHQFFQREGADLYCSVPISMTTAALGGTFDVTTLDGTKSRVTVPEGTQPGKQFRLKGKGMPVLRSAQMGDLYIQIQIETPQKLTKRQRELLQEFDQISSKENNPESTGFFARMKEFFEG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Aliivibrio salmonicida (strain LFI1238)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.395 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDETAPEKFKEVKVAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGGFGGGQGDFGDIFGDVFGDIFGGGRRGGQQRAQRGSDLRYNMELTLEEAVRGCEKDIEIPTLAACEPCDGTGAKKGTSSTTCSTCHGQGQVQMRQGFFAVQQACPTCHGKGKIIKDPCNSCHGDGRVQKTKTLNVKIPSGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVHVKEHNIFDRDGNNLYCEVPVSFTMAALGGEVEVPTLDGRVSLKVPLETQTGRMFRMRGKGVKGVRTHSAGDLIVKLIVETPVKLTKRQRELLKEFQESFDGKDAKKHNPKSEGFLSGVKNFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Geobacillus stearothermophilus
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.638 kDa
Sequence
MAKRDYYEILGVSKNATKEEIKKAYRKLSKKYHPDVNKEPDAAEKFKEIKEAYEVLSDDQKRAHYDQFGQADPNQGFGGFRSDDFDLGGFSGFGGFEDIFNTFFGGGRRRNPNAPRAGADLQYTMTLTFEEAAFGKETDIEIPSEETCNTCHGTGAKPGTKPETCPHCHGAGQISTEQSTPFGRIVNRRTCPYCGGTGQYIKEKCTTCGGTGRVKRRKKIHVKIPAGIDDGQQLRVAGQGERGLTVGRREIYILSFMWSRMSFLNVTAMIFIAKCRLRLRKLRLGMKSKSRPFTGKLKLKIPAGTQTGTRLRLKGKGVPNVRGYGYGDQHVIVRVVTPTKLTEKQKQLLREFDQLGGSSMHHEPHDRFFDKVKKAFKPES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Geobacillus sp. (strain WCH70)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.141 kDa
Sequence
MAKRDYYEILGVSKNATKEEIKKAYRKLSKKYHPDINKEPDAAEKFKEIKEAYEVLSDDQKRAHYDQFGHADPNQGFGGFRSDDFDFGGFSGFGGFEDIFSTFFGGGRRRDPNAPRAGADLQYTMTLTFEEAAFGKETDIEIPREETCDTCHGTGAKPGTKKETCSYCHGTGQISTEQSTPFGRIVNRRTCPYCGGTGQYIKEKCTTCGGTGRVKKRKKIHVKIPAGIDDGQQLRVAGQGEPGINGGPPGDLYIVFHVEPHEFFERDGDDIYCEIPLTFAQAALGDEIEVPTLHGKVKLKIPAGTQTGTKFRLKGKGVPNVRGYGYGDQHVIVRVVTPTKLTEKQKQLLREFDQLGGSSMHQGPYGRFFDKVKKAFKGES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Geobacillus thermoglucosidasius
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.257 kDa
Sequence
MAKRDYYEILGVSKNATKEEIKKAYRKLSKKYHPDINKEPDAAEKFKEIKEAYEVLSDDQKRAHYDQFGHADPNQGFGGFRSDDFDFGGFSGFSGFDDIFSTFFGGGRRRDPNAPRAGADLQYTMTLTFEEAVFGKETDIEIPREETCNTCHGTGAKPGTKKETCSYCHGTGQISTEQSTPFGRIVNRRTCPYCGGTGQYIKERCTTCGGTGRVKRRKKIHVKIPAGIDDGQQLRVAGQGEPGINGGPPGDLYIVFHVEPHEFFERDGDDIYCEIPLTFAQAALGDEIEVPTLHGKVRLKIPAGTQTGTKFRLKGKGVPNVRGYGYGDQHVIVRVVTPTKLTEKQKQLLREFDQLGGSSMHQGPHGRFFEKVKKAFKGES

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Gluconobacter oxydans (strain 621H)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.026 kDa
Sequence
MATRIDYYESLEVSRTASQDELKKAFRKQAMRYHPDRNPGDDAAEQKFKEINEAYDVLKDEQKRAAYDRYGHDAFEGGMGGMGGGFGGGFAGAGGLGDIFDQMFGDMMGGRRDGGRRTGADVQVQVEITLMEAFTGVTKDVEVRTRVTCEACHGSGSADPKAGSSTCPTCHGAGKVRAQQGFFLVERPCPTCHGSGRTVANPCKVCHGTGTEAKTETISIDIPAGVEDGTRIRMAGKGEAGGEGVQPGDLYVHISVLSHDIFQRDGANIYCRVPLRMTQAALGTEVEVPVVDGGRSKVRIPAGTQTGETFRLRGKGFSVLRSSARGDMYIQVSVETPSHLTKRQRELLEEFEKEAGDDHAKGSPENSGFFAKVRDFFEGR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.916 kDa
Sequence
MAKRDYYETLGVAKNASEEDIKKAYRKLAMKHHPDRNQGDGAKKAEESFKEAKEAYEMLSDAQKRAAYDQYGHAGVDPNMGGRGAGGPEAYGGFAEAFGDIFGDIFGQNGQRRGPGGQQVYRGNDLSYAMEITLEEAARGKDTQIRIPSWDSCSTCDGTGAKPGTSAKTCPTCSGSGQVHLRQGFFSIQQTCPSCHGTGKIIPEPCTACNGAGRIKSNKTLEVKIPAGINEGMRIRSAGNGEPGTNGGPAGDLYIEIRIKAHDIFERDGDDLHCTIPIGIATATLGGAIEVPTLGGKAEIELPEGTQHGKTFRLRGKGIKGVRSSYPGDLYCHVAVETPIKLTEHQRKLLRELDESLKKGGERHSPNAKSWTDRVKDLFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.195 kDa
Sequence
MSKRDYYEILGVTKTATEGEMKVAFRKLAMTYHPDRNPGDKDAEIKFKEINEAYQCLSDGQKRAAYDRFGHAAFSQGGGGPGFGNEFGDFMSDIFDNFFGDGRGGGGARGRGGTPGRERGADLRYNLEITLEEAFTGKAETIKIPTSITCEVCDGSGAKPGSKPRTCPTCAGYGRVRAAQGFFAIERTCPNCHGRGEIVDDPCTACQGAGRVNRERTLSINVPAGVDDGLRIRLAGEGESGLRGGPAGDLYVFLSIKQHEFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSQTQVRIPAGTQTAKQFRIKGKGMPVLRSREVGDLYIQVFVETPQNLTKRQRELLQEFDLSASPENHPESAGFFSKVRDFFGGAVRP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bartonella quintana (strain Toulouse)
Length
380 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.171 kDa
Sequence
MKVDYYEILGVTRECDDKKLKSAFRKLAMQYHPDRNAGDKEAERRFKEIGEAYEVLKDPQKRAAYDRFGHAAFENNNQGGGNPFGGFAAGGFSDIFEDFFGEIMGGGHRKRSDGRERGADLSYNMEVTLEEAFSGKTAQINIPSSIVCDSCEGSGAKKGSKPQICGTCHGAGRVRAAQGFFSIERTCHACNGRGEVITDPCPKCQGTRRVEKNRSLSVNIPAGIEDGTRIRLSGEGDAGIRGGPNGDLYIFLSVKPHEFFQREGADLHCRIPLSMVTAALGGEFEVSDLDGIKARVKIPEGTQNGRQFRLKGKGMPMLRRQQVRGDLYIHITIETPQKLTQEQRELLQKFEKLSNHENSPQSHGFFSRMKEFFENISGQN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Legionella pneumophila (strain Paris)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.28 kDa
Sequence
MEQRDYYELLEVSRNASDAEIKKAYRRLAMKYHPDRNPGDTSAEEKFKEIQKAYNILSDKQKRAAYDQFGHAGVDPSMGGGPGGFGGFGGFGDVFEDIFENIFSGGRGHGRQSRGQRGADLQFNVQLTLEEAAIGKEVEITVPRHGTCTVCEGSGAKKGTSPKTCETCQGMGQVRIQQGFFSIQQTCPTCHGEGKIISDPCASCHGQGRVRESKKINVKIPAGVDNGDRVRLSGEGEAGVHGGGSGDLYVQISLKKHAIFERHENDLHCEVPISFATAALGGSIEVPTLEGRVTLKIPAETQTGKVFRLRSKGMKSVRGYGQGDLLCKVVVETPVNLSREQKELLNKLQDSLENAKGTHSPKTSSWFAGVKKFFEDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Legionella pneumophila (strain Corby)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.28 kDa
Sequence
MEQRDYYELLEVSRNASDAEIKKAYRRLAMKYHPDRNPGDTSAEEKFKEIQKAYNILSDKQKRAAYDQFGHAGVDPSMGGGPGGFGGFGGFGDVFEDIFENIFSGGRGHGRQSRGQRGADLQFNVQLTLEEAAIGKEVEITVPRHGTCTVCEGSGAKKGTSPKTCETCQGMGQVRIQQGFFSIQQTCPTCHGEGKIISDPCASCHGQGRVRESKKINVKIPAGVDNGDRVRLSGEGEAGVHGGGSGDLYVQISLKKHAIFERHENDLHCEVPISFATAALGGSIEVPTLEGRVTLKIPAETQTGKVFRLRSKGMKSVRGYGQGDLLCKVVVETPVNLSREQKELLNKLQDSLENAKGTHSPKTSSWFAGVKKFFEDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.28 kDa
Sequence
MEQRDYYELLEVSRNASDAEIKKAYRRLAMKYHPDRNPGDTSAEEKFKEIQKAYNILSDKQKRAAYDQFGHAGVDPSMGGGPGGFGGFGGFGDVFEDIFENIFSGGRGHGRQSRGQRGADLQFNVQLTLEEAAIGKEVEITVPRHGTCTVCEGSGAKKGTSPKTCETCQGMGQVRIQQGFFSIQQTCPTCHGEGKIISDPCASCHGQGRVRESKKINVKIPAGVDNGDRVRLSGEGEAGVHGGGSGDLYVQISLKKHAIFERHENDLHCEVPISFATAALGGSIEVPTLEGRVTLKIPAETQTGKVFRLRSKGMKSVRGYGQGDLLCKVVVETPVNLSREQKELLNKLQDSLENAKGTHSPKTSSWFAGVKKFFEDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Legionella pneumophila (strain Lens)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.271 kDa
Sequence
MEQRDYYELLEVSRNASDAEIKKAYRRLAMKYHPDRNPGDTSAEEKFKEIQKAYNILSDKQKRAAYDQFGHAGVDPSMGGGPGGFGGFGGFGDVFEDIFENIFSGGRGQGRQSRGQRGADLQFNVQLTLEEAAIGKEVEITVPRHGTCTVCEGSGAKKGTSPKTCETCQGMGQVRIQQGFFSIQQTCPTCHGEGKIISDPCASCHGQGRVRESKKINVKIPAGVDNGDRVRLSGEGEAGVHGGGSGDLYVQISLKKHAIFERHENDLHCEVPISFATAALGGSIEVPTLEGRVTLKIPAETQTGKVFRLRSKGMKSVRGYGQGDLLCKVVVETPVNLSREQKELLNKLQDSLENAKGTHSPKTSSWFAGVKKFFEDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Legionella pneumophila
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.28 kDa
Sequence
MEQRDYYELLEVSRNASDAEIKKAYRRLAMKYHPDRNPGDTSAEEKFKEIQKAYNILSDKQKRAAYDQFGHAGVDPSMGGGPGGFGGFGGFGDVFEDIFENIFSGGRGHGRQSRGQRGADLQFNVQLTLEEAAIGKEVEITVPRHGTCTVCEGSGAKKGTSPKTCETCQGMGQVRIQQGFFSIQQTCPTCHGEGKIISDPCASCHGQGRVRESKKINVKIPAGVDNGDRVRLSGEGEAGVHGGGSGDLYVQISLKKHAIFERHENDLHCEVPISFATAALGGSIEVPTLEGRVTLKIPAETQTGKVFRLRSKGMKSVRGYGQGDLLCKVVVETPVNLSREQKELLNKLQDSLENAKGTHSPKTSSWFAGVKKFFEDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermosipho africanus (strain TCF52B)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.499 kDa
Sequence
MAKKDYYEILGVSRNASQEEIRQAYKQLIKKWHPDRNHQNRKEAEEKFKEIQEAYEVLSDPEKRAMYDRFGYVGDVPPNAGSGGGFGGFGGFGGFEDIFKDFGDFINNDIFNIFFGDQRTSSRQKQRRAKRGEDINITVDVPFEQVFTGTTIPIEYDRYEVCSHCNGEGVEPGSGWVSCPKCHGTGVVREERRTFLGVIVNQYTCNQCGGTGKIPGETCHVCGGSGRIRKRHRVEVKIPAGVDNGTVIRVQGKGNAGYNGGGYGDLYVNVRITGHIDFERRGNDLIKEIKIDYVEAILGTKVKIKMPDGRVKEVKIPSGVQDGENIYVYGEGVPDMRTGRRGDLILKIKVDIPKRVSRSEKKLLKEIAKLRGKDVDEEE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.084 kDa
Sequence
MPASKRDYYEVLGVDKKASNDDIKKAYRKLAIKYHPDKNQGDKAAEEKFKEATEAYEILIDEKKRSMYDQFGHAGVDGMSGGGGYDPSAFQGFEDIFGGSFSDIFENLFGGGFSSRSSGFGGRHAGPVRGSNLRYDLQISFVDAVYGKKAELSYTRNEKCSECHGTGSESGSSKRMCPDCKGTGQVRQSTGFFSISRPCPTCGGEGSIIEKPCKKCGGNGLERKKQRIIVTIPAGVENGKRITIPSQGNAGQAGGDYGDLFVFIFVQAHPYFERNGIDLYCAVPISMTQAALGGEINIKSLDEKTLRLKIPAGTQNGKLLRIRGEGVPTGIGRKGDLYIQIQVQIPSKLSSNSKKLLQEISAIEGENENPNLIPLKDLP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.201 kDa
Sequence
MAKKDYYEILGVPKTADEREIKKAYKRLAMKFHPDRNQGDKEAEAKFKEIKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGFGNGADFSDIFGDVFGDIFGGGRGRRASRGADLRYNMELTLEEAVRGVTKEIRIPTLEECEVCHGSGAKPGSQPQTCPTCHGAGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNSCHGHGRIEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEQGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNDRQKALLQELQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.931 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKHHPDRNPDNKEAEEKFKEVKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGGGFGGGGFAEAFGDIFGDIFGQAAGGGRRGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCEHCHGNGAEPGSSVETCPTCNGVGQVRVSQGFFTMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKQHPVFERDGDDLHCQMPISFATAALGGDIEVPTLGGRASFPVPEGTQAGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKDILRQFDRSVHEGGSRHSPQEQSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.065 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKYHPDRNPDSKESEEKFKEVKEAYEMLSDAEKKAAYDQYGHAGVDPNMAGGFGGGQGYGGFAEAFGDIFGDIFGQQAGGGRRGGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFSMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKAHPVFERDGDDLHCQMPISFATAALGGDLEVPTLNGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKDMLRQFDRSVHEGGSRHSPQEQSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.252 kDa
Sequence
MSKRDYYEVLGVEKSASERDIKKAYKRLAMKYHPDRTQGDKAMEEKFKEVQEAYEILTDSQKRAAYDQYGHAGVDPNRGHGGGHGAGDFGDIFGDVFGDIFGGGRGGGRQSRAARGSDLRYNLELSLEEAVRGKSVEIRVPTLAECDTCDGSGAKKGSSAKTCTTCHGQGQVQMRQGFFAVQQACPTCGGKGKIITDPCDVCHGQGRVEKTKTLSVKVPAGVDTGDRIRLSNEGEAGENGAPAGDLYVQVHVKQHKIFERDGNNLYCEVPLSFTRAAIGGEIEVPTLEGKVKLKVTPETQTGKMFRLRNKGVKSVRSGSVGDLICKVVIETPVNLNSRQKELLQELEESMGKGKETAKNRPKESGFFDGVKKFFDDLTN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.201 kDa
Sequence
MAKKDYYEILGVPKTADEREIKKAYKRLAMKFHPDRNQGDKEAEAKFKEIKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGFGNGADFSDIFGDVFGDIFGGGRGRRASRGADLRYNMELTLEEAVRGVTKEIRIPTLEECEVCHGSGAKPGSQPQTCPTCHGAGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNSCHGHGRIEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEQGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNDRQKALLQELQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.931 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKHHPDRNPDNKEAEEKFKEVKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGGGFGGGGFAEAFGDIFGDIFGQAAGGGRRGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCEHCHGNGAEPGSSVETCPTCNGVGQVRVSQGFFTMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKQHPVFERDGDDLHCQMPISFATAALGGDIEVPTLGGRASFPVPEGTQAGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKDILRQFDRSVHEGGSRHSPQEQSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.065 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKYHPDRNPDSKESEEKFKEVKEAYEMLSDAEKKAAYDQYGHAGVDPNMAGGFGGGQGYGGFAEAFGDIFGDIFGQQAGGGRRGGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFSMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKAHPVFERDGDDLHCQMPISFATAALGGDLEVPTLNGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKDMLRQFDRSVHEGGSRHSPQEQSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.252 kDa
Sequence
MSKRDYYEVLGVEKSASERDIKKAYKRLAMKYHPDRTQGDKAMEEKFKEVQEAYEILTDSQKRAAYDQYGHAGVDPNRGHGGGHGAGDFGDIFGDVFGDIFGGGRGGGRQSRAARGSDLRYNLELSLEEAVRGKSVEIRVPTLAECDTCDGSGAKKGSSAKTCTTCHGQGQVQMRQGFFAVQQACPTCGGKGKIITDPCDVCHGQGRVEKTKTLSVKVPAGVDTGDRIRLSNEGEAGENGAPAGDLYVQVHVKQHKIFERDGNNLYCEVPLSFTRAAIGGEIEVPTLEGKVKLKVTPETQTGKMFRLRNKGVKSVRSGSVGDLICKVVIETPVNLNSRQKELLQELEESMGKGKETAKNRPKESGFFDGVKKFFDDLTN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.058 kDa
Sequence
MADKRDYYEVLGVDKNASDAELKKAYRNLAKKYHPDVNPGDTTAEAKFKEVNEAYEILSDSQKRSRYDQFGHAGTDPNGFGGAGGFSTDFDFGGIGDIFETFFGGSGFGGRSKTRRGPQKGADIKYSTEISFEEAAFGVEREINVSKMEVCSKCTGSGAKPGSNVTTCNHCNGTGQVQIKQNTPFGQFINTKTCDACKGEGKIITEPCPACNGKGRLRSTKKIKIDIPAGIDDGQTISLRGGGDPGVKGGPNGDLYVNIRVKPHPLFTRQGNNVVCEVPITFTQAALGAELEVPTLDGKVKYTVPEGTQTGSVFRLKGKGIPYLRGNGRGDQYVKVNIEVPKKLNDKQKALLREFAEISGDDSHEQRKGFFDKMKDAFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.725 kDa
Sequence
MAKKDYYEILGLDKGASDQDIKKAFRKLALKYHPDRNPNDKKAEEKFKEINEAYQVLTDPQKKAQYDQFGTTDFNGGGFQGGFGGFDFSDLGGFGDIFDSFFGGGFSSGRRKNGPERGSDLEYTLSLTFEEAVFGVEKEISVTRNERCETCNGTGAKKGSHPHTCDKCNGTGQVRHQRSTPLGNFVTMTTCDKCGGRGTIIKNPCEECRGKGIVRKHRKIKVKVPAGVDTGNIIPIRGQGEHGKNGGPSGDLYINLRVSPHSKFKRKGFDIYLDAHISFGKAALGTSLKVPSIDGDVKYEIPPGTQPGTVFRLKGKGVPKVDGRGRGDQYVNVIVDIPKNLNEKQKEALMMFMEASGEIQPRDVEKKSFIDKIFKNDSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Colwellia maris
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.995 kDa
Sequence
MSKRDYYETLEVSQDASEKEIKKAYKKLAMKYHPDRTQGDKSKEETFKEVKEAYEILNDDQKRAAYDQYGHAAFEQGGHGGGGGGHGGGFGQDFGDIFGDIFGGGGGGGRGRQRQQRGSDLRYNVELSLEDAVKGKSLEIKVPTYVSCEPCDGSGAKKGTSAKTCSTCHGHGQVQMRQGLFAVQQTCPTCSGKGKVIADKCTSCRGQGRVEKTKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVNVRDHDIFVRDENHLYCEVPISFVTASLGGEIEVPTLGGKVKLKVPKETQTGKMFRLRGKGVKSVRSTSTGDLMCKVVIETPVNLSGDQADLLRQLEEKMASSSKKHSPKETGFFDGVKKFFDDLKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.728 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKHHPDRNPGNKDAEGHFKEVKEAYEMLSDSQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGGRAGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEICHGSGAKPGTKPETCPTCSGSGSVRMSQGFFSIQQTCPKCHGTGTYIPEPCGHCHGAGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKQHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTEPQRDLLKQFEKALVEGGSRHSPQSKSWFDRVKSFFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.212 kDa
Sequence
MAKQDYYESLGVAKSADDREIKKAYKRLAMKYHPDRNPGDSEAEAKFKEIKEAYEILIDSQKRAAYDQYGHAAFEQGGMGGGGGGGFGGGGADFGDIFGDVFGDIFGGGRRQRASRGSDLRYNMELSLEEAVRGVTKEIRIPALEECDVCHGNGAKPGSSPITCPTCHGNGQVQMRQGFFTVQQACPHCHGRGKIIKDPCIKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGDHGAPSGDLYVQVQVKAHPIFQREENNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPAETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVNLNERQRQLLQELDESFGGPSGERNSPRSKNFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.832 kDa
Sequence
MAKRDYYETLGCDRGADDTVLKASYRKLAMKWHPDRSQGNGEAEVMFKEVNEAYEVLKDPQKRAAYDRFGHAAFENGGGGGPGFGNDFASSFADIFDDLFGGAMNRGRGGGQQRGRGADLRYNMEITLEEAFSGKTAQIKIPTSVSCETCSGTGAKPGTQPKACRMCGGAGKIRHAQGFFTLERTCPNCQGRGSVIEDPCSDCGGAGRVTRERNLSVQIPAGVEDGTRIRLGGEGEAGVRGGAAGDLYIFLSIEPHTFFQREGADLYCRVPISMVTAALGGTVEVPTIDGDKSKVKIPEGTQSQKRFRLSGKGMPIMRARNHGDMYVQVVVETPQKLTKRQKELLAEFEKDSSGETHPESTGFFAKVKEFFQGAAGEGA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRKSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRQSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRQSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pestis
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRQSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRQSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRQSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia pestis (strain Pestoides F)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.279 kDa
Sequence
MAKRDYYEVLGVSRDAEEREIKKAYKRLAMKFHPDRQSEDKNAEEKFKEAKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGFGGGGGGADFSDIFGDVFGDIFGGGRRQQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLDECDVCHGSGAKPGSSPVTCPTCHGAGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMRGKGVKSVRGGSQGDLLCRVVVETPVSLSEKQKQLLRELEESFVGAAGEKNSPRAKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Sinorhizobium fredii (strain NBRC 101917 / NGR234)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.433 kDa
Sequence
MKRDLYETLGVKKNADEKELKSAFRKLAMKYHPDRNPGDQEAEKSFKEINEAYETLKDPQKRAAYDRYGHAAFEQGGMGAGFGNGFAGGSAGGFSDIFEDIFGEMMGGRQRRSSGGRERGADLRYNMEITLEEAYSGKTAQIRVPTSVTCDVCTGSGAKPGTSPKTCATCQGSGRIRAAQGFFSIERTCPTCGGRGQTITDPCTKCHGQGRVTEERTLSVNIPTGIEDGTRIRLSGEGEAGLRGGPAGDLYIFLSVKPHEFYQRDGADLYCSVPISMTTAALGGKFDVTTLDGTKSRVTVPEGTQAGKQFRLKGKGMPVLRSNQTGDLYIQIQIETPQKLTKRQRELLQEFEQISSKENNPQSTGFFSRMKDFFDTLSE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain JH1)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain USA300)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.253 kDa
Sequence
MSKRDFYEVLGVSRDASERDIKKAYKRLAMKFHPDRNQGDDTAAEKFKEVKVAYEILTDAQKRSAYDQYGHAAFEQGGMGGGGFGGGGADFGDIFGDVFGDIFGGGRRGGQQRAQRGSDLRYNMELTLEEAGRGCDKEIEVPTLVSCDPCEGTGAKKGTSSTTCSTCHGQGQVQMRQGFFAVQQACPTCHGKGKIIKDPCNSCHGEGRVHKTKTLNVKIPSGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVHVKEHNIFERDGNNLYCEVPVSFTMAALGGEVEVPTLDGRVSLKVPLETQTGRMFRMRGKGVKGVRTHSAGDLIVKLIVETPVKLTKRQKELLQEFQESFDGKDAKKHNPKSEGFLSGVKNFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Anaplasma marginale (strain Florida)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.961 kDa
Sequence
MSGNDYYEILEVSRNASAEEIKKSYRKMVFKYHPDKNPGDKKAEEKFKKISEAYEVLSNPEKRAAYDRYGHSTFTSGGASGFDFTSGFSTDFSDIFQDFFGGGFGKSQRASSREHLRGSDLRYDVEVSLEDAFKGIKVPISYVTNVKCSSCSGIGSEGAVNSVKCGNCNGAGSVRTRKGFLTIEEVCNVCNGEGEVIKNKCRRCGGSGRVRNEVSLLVTVPKGIETGNKVRVNGKGEAGFRGAQEGDLYVYIRVKEHKFFTRRSSDLHCSVPIKMTIAALGGEIEMPSIDGSWTKLKIPEGTQSGDQIRMRGKGMPEVNSKDRRGDMYVHVTVETPVKLTKQQVDLLKKFEEESSANCSPKYQGFFQKIKDIWRDISSG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Anaplasma marginale (strain St. Maries)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.961 kDa
Sequence
MSGNDYYEILEVSRNASAEEIKKSYRKMVFKYHPDKNPGDKKAEEKFKKISEAYEVLSNPEKRAAYDRYGHSTFTSGGASGFDFTSGFSTDFSDIFQDFFGGGFGKSQRASSREHLRGSDLRYDVEVSLEDAFKGIKVPISYVTNVKCSSCSGIGSEGAVNSVKCGNCNGAGSVRTRKGFLTIEEVCNVCNGEGEVIKNKCRRCGGSGRVRNEVSLLVTVPKGIETGNKVRVNGKGEAGFRGAQEGDLYVYIRVKEHKFFTRRSSDLHCSVPIKMTIAALGGEIEMPSIDGSWTKLKIPEGTQSGDQIRMRGKGMPEVNSKDRRGDMYVHVTVETPVKLTKQQVDLLKKFEEESSANCSPKYQGFFQKIKDIWRDISSG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodospirillum centenum (strain ATCC 51521 / SW)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.903 kDa
Sequence
MSKRDYYEVLGVQKGASADDLKKAYRKLAMQYHPDRNQGDKAAEQKFKEISEAYDVLKDDQKRAAYDRFGHAAFENGRGGPGAGAAGFDFNFGSGFADIFDEMFGEFMGRGRAGQTSNRGADLRYNLEITLEDAFKGATTTVRVPTSVACESCNGTGAEGGSTPIACPTCNGHGKVRAQQGFFTIERTCPACHGVGRVIKDPCRTCGGQGRVRKEKTLSVNIPAGVEDGTRIRLAGEGEAGLRGGPPGDLYIFLAIAPHRFFQRDGANLQCRVPIPMTTAALGGSVEVPTIDGSRAKIAIPAGTQTGHQFRLKGKGMSVLRSPARGDLYIQVVVETPVNLTKKQQELLREFEKAGQDGLHPESEGFFAKVKELWADLKD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodopseudomonas palustris (strain HaA2)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.838 kDa
Sequence
MSTTKRCYYETLEVERSADESTLKSAFRKLAMKWHPDRNPGDASSEIKFKEINEAYEVLKDGDKRAAYDRYGHAAFEQGMGGGGPGFGAGFASSFSDIFEDLFGMAGQRGRGTGRERGADLRYNMEITLEDAYKGKTAQIEIPVSVTCESCSGTGAKAGTKPKTCSTCGGAGRVRQAQGFFTLERTCPSCQGRGQIIEDPCPSCTGSGRVTKERTLSVNIPQGVEDGTRIRLAGEGEAGVRGGPPGDLYIFLSLASHAIFQRDGADLHCRVPISMVTAALGGEFEVPTIERGKTKVKVPSGTQTGRRFRIAGKGMPVLRSRQVGDMYVQVAVETPQNLTKKQQELLAEFEKLSSGATQPEAAGFFSKVKDFFGSRANTP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.992 kDa
Sequence
MSTTKRCYYETLEVERNADDSTLKSAFRKLAMKWHPDRNPGDPQCEIKFKEINEAYEVLKDGDKRAAYDRYGHAAFEQGGFGGGAGFGAGFASSFSDIFEDLFGMAAQRGRGTGRERGADLRYNMEITLEDAFKGKTAQIEIPVSVTCEACSGTGAKAGTKPKTCSTCGGAGRVRQAQGFFTLERTCPSCQGRGQTIEDPCPSCTGSGRVTKERTLSVNIPQGVEDGTRIRLAGEGEAGLRGGPPGDLYIFLSLANHAIFQRDGADLHCRVPISMVTAALGGEFEVPTIDRGKTKVKVPSGTQTGRRFRIAGKGMPVLRSRQVGDMYVQVVVETPQNLTKKQQELLAEFEKLSSGETQPEAVGFFSKVKEFFGSRASAP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodopseudomonas palustris (strain BisB18)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.664 kDa
Sequence
MSTTKRCYYETLEVDRSADDSSLKAAFRKLAMKWHPDRNPGDASSESRFKEINEAYEVLKDGDKRAAYDRYGHAAFEQGGAGGPGFGAGFASSFSDIFEDLFGMAGQRGGRGTGRERGADLRYNMEITLEDAFVGKTAQIEIPVSVTCESCSGTGAKAGTKPKTCSMCGGAGRVRQAQGFFTLERTCPGCQGRGQTIEDPCPACSGAGRIERERTLSVNIPQGVEDGTRIRLAGEGEAGLRGGPPGDLYIFLSLASHEFFQRDGADLHCRVPISMVAAALGGEIEVPTIDKGKSKVKVPSGTQSGRRFRIAAKGMPVLRSRQTGDMYVQVVVETPQNLTKRQQELLAEFEKLSSGATQPEAAGFFTKVKDFFGTRGAAS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodopseudomonas palustris (strain TIE-1)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.992 kDa
Sequence
MSTTKRCYYETLEVERNADDSTLKSAFRKLAMKWHPDRNPGDPQCEIKFKEINEAYEVLKDGDKRAAYDRYGHAAFEQGGFGGGAGFGAGFASSFSDIFEDLFGMAAQRGRGTGRERGADLRYNMEITLEDAFKGKTAQIEIPVSVTCEACSGTGAKAGTKPKTCSTCGGAGRVRQAQGFFTLERTCPSCQGRGQTIEDPCPSCTGSGRVTKERTLSVNIPQGVEDGTRIRLAGEGEAGLRGGPPGDLYIFLSLANHAIFQRDGADLHCRVPISMVTAALGGEFEVPTIDRGKTKVKVPSGTQTGRRFRIAGKGMPVLRSRQVGDMYVQVVVETPQNLTKKQQELLAEFEKLSSGETQPEAVGFFSKVKEFFGSRASAP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rhodopseudomonas sp. (strain No.7)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.992 kDa
Sequence
MSTTKRCYYETLEVERNADDSTLKSAFRKLAMKWHPDRNPGDPQCEIKFKEINEAYEVLKDGDKRAAYDRYGHAAFEQGGFGGGAGFGAGFASSFSDIFEDLFGMAAQRGRGTGRERGADLRYNMEITLEDAFKGKTAQIEIPVSVTCEACSGTGAKAGTKPKTCSTCGGAGRVRQAQGFFTLERTCPSCQGRGQTIEDPCPSCTGSGRVTKERTLSVNIPQGVEDGTRIRLAGEGEAGLRGGPPGDLYIFLSLANHAIFQRDGADLHCRVPISMVTAALGGEFEVPTIDRGKTKVKVPSGTQTGRRFRIAGKGMPVLRSRQVGDMYVQVVVETPQNLTKKQQELLAEFEKLSSGETQPEAVGFFSKVKEFFGSRASAP

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactococcus lactis subsp. lactis (strain IL1403)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.671 kDa
Sequence
MNNTEYYERLGVDKNASQDEIKKAYRKMSKKYHPDLNKEEGAEEKYKEVQEAYETLSDEQKRAAYDQYGEAGANGGFGGGGFGGASGFSGFGGGSGGFGGFEDIFSSFFGGGGAQVNPNAPRQGDDLQYRINLKFEEAIFGVEKQVKYNREELCHTCGGSGAKAGTHPETCHKCGGRGQINVVRDTPLGRMQTQVTCDVCNGTGKEIKEKCETCHGSGHEKVAHTVKVTVPAGVETGQKMRLQGQGDAGVNGGPYGDLYVVFQVEASDKFERDGAEIYYKMPMDFVQAALGDEIEVPTVHGNVKLKIPAGTQTGANFRLKGKGAPKLRGSGNGDQYVIINIVTPKNLNQAQKEALQAFAKASGVEVSGSGKKGFFDKFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactococcus lactis subsp. cremoris
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.84 kDa
Sequence
MNNTEYYERLGVDKNASQDEIKKAYRKMSKKYHPDLNKEEGAEDKYKEVQEAYETLSDEQKRAAYDQYGEAGRNGGFGGGGFGGASGFSGFGGRSGGFGGFEDIFSSFFGGGGAQVNPNAPRQGDDLQYRINLKFEEAIFGVEKQVKYNREELCHTCGGSGAKAGTHPETCHKCGGRGQINVVRDTPLGRMQTQTTCDVCHGTGKEIKEKSTTCHGSGHEKVAHTVKVTVPAGVETGQKMRLQGQGDAGVNGGPYGDLYVVFQVEASDKFERDGAEIYYKMPMDFVQAALGDEVEVPTVHGNVKLKIPAGTQTGANFRLKGKGAPKLRGSGNGDQYVIINIVTPKNMNQAQKEALQAFAKASGIEVSGSGQKGFFDKFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.686 kDa
Sequence
MNNTEYYERLGVDKNASQDEIKKAYRKMSKKYHPDLNKEEGAEDKYKEVQEAYETLSDEQKRAAYDQYGEAGANGGFGGGGFGGASGFSGFGGASGGFGGFEDIFSSFFGGGGAQVNPNAPRQGDDLQYRINLKFEEAIFGVEKQVKYNREELCHTCGGSGAKAGTHPETCHKCGGRGQINVVRDTPLGRMQTQTTCDVCHGTGKEIKEKCTTCHGSGHEKVAHTVKVTVPAGVETGQKMRLQGQGDAGVNGGPYGDLYVVFQVEASDKFERDGAEIYYKMPMDFVQAALGDEVEVPTVHGNVKLKIPAGTQTGANFRLKGKGAPKLRGSGNGDQYVIINIVTPKNMNQAQKEALQAFAKASGIEVSGSGKKGFFDKFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactococcus lactis subsp. cremoris (strain SK11)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.744 kDa
Sequence
MNNTEYYERLGVDKNASQDEIKKAYRKMSKKYHPDLNKEEGAEDKYKEVQEAYETLSDEQKRAAYDQYGEAGANGGFGGGGFGGASGFSGFGGASGGFGGFEDIFSSFFGGGGAQVNPNAPRQGDDLQYRINLKFEEAIFGVEKQVKYNREELCHTCDGSGAKAGTHPETCHKCGGRGQINVVRDTPLGRMQTQTTCDVCHGTGKEIKEKCTTCHGSGHEKVAHTVKVTVPAGVETGQKMRLQGQGDAGVNGGPYGDLYVVFQVEASDKFERDGAEIYYKMPMDFVQAALGDEVEVPTVHGNVKLKIPAGTQTGANFRLKGKGAPKLRGSGNGDQYVIINIVTPKNMNQAQKEALQAFAKASGIEVSGSGKKGFFDKFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella paratyphi C (strain RKS4594)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella typhi
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity). Necessary for invasion of epithelial cells, secretion of invasion proteins and proliferation within macrophages.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella agona (strain SL483)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella choleraesuis (strain SC-B67)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella dublin (strain CT_02021853)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella heidelberg (strain SL476)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella newport (strain SL254)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.313 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mannheimia haemolytica
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.185 kDa
Sequence
MAKKDYYEVLGLSKGASEKDIKRAYKRLAAKHHPDKNQGSKESEEKFKEITEAYDVLTDSEKKAMYDQYGHAAFEQGGAGAGGFGGFGGGGFGGFEDIFSEMFGGGFGGGGRRQRVVRGDDLRYDIEITLEEAVKGCKKDIRIHTLAECDTCHGTGAEAGSKVETCSHCHGSGRIRRQQGFFVTDAVCPSCHGTGKRIEKPCRSCHGDGRVHKAKNLSVTIPAGVDTGNQLRLSREGAAGENGAPAGDLYVVIPVKEHDIFERDGSNLYCEVPIIFTLAALGGEIEMPTLDGQLKLKFRQKLQPVNYSVLRGKGVTSPRGGYAGDLICKVVVETPVNLTEEQKALLRQFEESLEGQGKHRPKHEGFFDGVKKFFDNLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain JH9)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.75 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNASQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain COL)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain Newman)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain N315)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain MRSA252)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.747 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINDQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain MSSA476)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain USA300 / TCH1516)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.655 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRATIDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGSQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus aureus (strain MW2)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.761 kDa
Sequence
MAKRDYYEVLGISKDASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDNKRASYDQFGHDGPQGFGGQGFNGSDFGGFSGFGGGGFEDIFSSFFGGGRQRDPNAPQKGDDLQYTMTLTFEEAVFGTTKEISIRKDVTCETCHGDGAKPGTSKKTCSYCNGAGHVAVEQNTILGRVRTEQVCPKCNGSGQEFEEACPTCHGKGTENKTVKLEVKVPEGVDNEQQIRLAGEGSPGVNGGPAGDLYVVFRVKPSETFKRDGDDIYYKLNVSFPQAALGDEIKIPTLNNEVMLTIPAGTQTGKQFRLKEKGIKNVHGYGYGDLYVDIKVVTPTKLTDRQKELMKEFAQLNGEEINEQPSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus agalactiae serotype III (strain NEM316)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.684 kDa
Sequence
MNNTEFYDRLGVSKDASQDEIKKAYRRMSKKYHPDINKETGAEEKYKEVQEAYETLSDTQKRAAYDQYGAAGANGGFGGFDGGGFGGFDGGGFGGFEDIFSSFFGGGGMRNPNAPRQGDDLQYRVNLSFEEAIFGAEKEVSYNRESSCHTCSGSGAKPGTSPVTCQKCHGSGVINVDTQTPLGTMRRQVTCDVCQGSGQEIKEKCPTCHGTGHEKKTHKVSVKIPAGVETGQQIRLTGQGEAGFNGGPYGDLFVIINVLPSQQFERNGSTIYYTLKISFVQAALGDTIDIPTVHGAVEMSIPAGTQTGKTFRLRGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQKEALHAFAEASGDKMVHPKKKGFFDKVKDALDVD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Length
379 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.67 kDa
Sequence
MNNTEFYDRLGVSKDASQDEIKKAYRRMSKKYHPDINKETGAEEKYKEVQEAYETLSDTQKRAAYDQYGAAGANGGFGGFDGGGFGGFDGGGFGGFEDIFSSFFGGGGMRNPNAPRQGDDLQYRVNLSFEEAIFGAEKEVSYNRESSCHTCSGSGAKPGTSPVTCQKCHGSGVINVDTQTPLGTMRRQVTCDVCQGSGQEIKEKCPTCHGTGHEKKTHKVSVKIPAGVETGQQIRLTGQGEAGFNGGPYGDLFVIINVLPSQQFERNGSTIYYTLNISFVQAALGDTIDIPTVHGAVEMSIPAGTQTGKTFRLRGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQKEALHAFAEASGDKMVHPKKKGFFDKVKDALDVD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.424 kDa
Sequence
MAGDFYEILGVSRDCGKDELKRAYRRLARQYHPDVNKDPGAEEKFKEINRAYEVLSEPETRARYDRFGEAGVSGAGAAGADYGDMGGFADIFETIFSGFGGMGTGATGGGRRRSGPMRGDDLRLDLKLDFKEAIFGGEKEIRIPHLETCKTCSGSGAKAGTSANTCGTCNGTGQVRRATRTPFGSFAQVSVCPTCNGEGQVIAEKCESCGGAGRKQETKKLKITIPAGVDSGTRLRVSREGDAGVKGGPPGDLYVYLAVNADKEFRRDGTNILSEIEISYLQAILGDTVKVKTVDGTEDLTIPAGLQPNKVLILEGKGVPKLGNPVSRGDHLITVKVMIPTKVSREEKELLHQLAKLKGTEHSKGGFEGLLGNLFHNK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.57 kDa
Sequence
MADFYDTLGVNRNADADSLKRAYRRLARQYHPDINKEAGAEERFKEIGRAYEVLGDPEKRARYDQFGEAGLGGSAGMPDMGDMGGFADIFETFFSGFGGPGSSGARTQRRGPQQGDDLRYDLTIDFNQAVFGQEREIKIPHLETCDVCRGTGAKPGTGPTTCSTCGGAGQVRRATRTPFGSFTQVSDCPTCSGSGQVISDSCQSCGGQGVKQVRKKLRINIPAGVDTGTRLRVSGEGNAGPRGGPSGDLYVFLKVKSHARLKRDGLNIHSEVNVSYLQAILGDTIEVDTVDGPTTLQIPSGTQPSAVLILDNKGIPKLGNPVARGNHCISVNIKIPSRLTDDEKILLEKLAIYYSAKGPQNHHHNSGLFSRLFKSNAS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Proteus mirabilis (strain HI4320)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.391 kDa
Sequence
MAKRDFYEVLGLSKTADEKEIKRAYKRLAMKYHPDRNQGDKDSESKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGFGGQGGGGFGGADFSDIFGDVFGDIFGGGRRQQRAARGSDLQYNMDLTLEEAVRGITKEIRIPTLETCDKCHGSGAKEGTSAETCSTCHGAGQVHLRQGFFTVQQPCPTCHGRGKVIKEPCSKCHGDGRVERYKTLSVKIPAGVDTGDRIRLSGEGEAGEQGAPAGDLYVQVHVRQHHIFERDGNNLYCEVPINFAVAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMKGKGVKSVRSHGVGDLMCRVVVETPVKLNEKQKQLMEQLGESFGGKGGEKNTPRSKSFLDGVKKFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.415 kDa
Sequence
MADYYDLLGVSKDADGDTLKRAYRRLARQYHPDINKDPGAEDRFKEIGRAYEVLSDPQTRGRYDQFGEAGLGGAAGMPDVGDMGGFADLFETFFSGFGGAGGSGGARPRRRGPQQGDDLRYDLKIDFEQAVFGQEREIKIPHLETCDTCNGTGAKVGSGPTTCSTCGGVGQVRRATRTPFGSFTQVAECPSCEGTGQVIADPCPACAGQGVRQVRKKLRINIPAGVDTGTRLRVAGEGNAGLRGGPSGDLYVFLTVKSHPQLRRDGITVLSEVNVSYLQAILGDIIEVDTVDGNTSLEIPAGTQPNAVLTLENKGIPKLGNPVARGNQRISINVKLPIRLSDEERGLLEELAGHHSAKGRQHHHHNSGLFARLFGQKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.57 kDa
Sequence
MADFYDTLGVNRNADADSLKRAYRRLARQYHPDINKEAGAEERFKEIGRAYEVLGDPEKRARYDQFGEAGLGGSAGMPDMGDMGGFADIFETFFSGFGGPGSSGARTQRRGPQQGDDLRYDLTIDFNQAVFGQEREIKIPHLETCDVCRGTGAKPGTGPTTCSTCGGAGQVRRATRTPFGSFTQVSDCPTCSGSGQVISDSCQSCGGQGVKQVRKKLRINIPAGVDTGTRLRVSGEGNAGPRGGPSGDLYVFLKVKSHARLKRDGLNIHSEVNVSYLQAILGDTIEVDTVDGPTTLQIPSGTQPSAVLILDNKGIPKLGNPVARGNHCISVNIKIPSRLTDDEKILLEKLAIYYSAKGPQNHHHNSGLFSRLFKSNAS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Proteus mirabilis (strain HI4320)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.391 kDa
Sequence
MAKRDFYEVLGLSKTADEKEIKRAYKRLAMKYHPDRNQGDKDSESKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGFGGQGGGGFGGADFSDIFGDVFGDIFGGGRRQQRAARGSDLQYNMDLTLEEAVRGITKEIRIPTLETCDKCHGSGAKEGTSAETCSTCHGAGQVHLRQGFFTVQQPCPTCHGRGKVIKEPCSKCHGDGRVERYKTLSVKIPAGVDTGDRIRLSGEGEAGEQGAPAGDLYVQVHVRQHHIFERDGNNLYCEVPINFAVAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMKGKGVKSVRSHGVGDLMCRVVVETPVKLNEKQKQLMEQLGESFGGKGGEKNTPRSKSFLDGVKKFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.415 kDa
Sequence
MADYYDLLGVSKDADGDTLKRAYRRLARQYHPDINKDPGAEDRFKEIGRAYEVLSDPQTRGRYDQFGEAGLGGAAGMPDVGDMGGFADLFETFFSGFGGAGGSGGARPRRRGPQQGDDLRYDLKIDFEQAVFGQEREIKIPHLETCDTCNGTGAKVGSGPTTCSTCGGVGQVRRATRTPFGSFTQVAECPSCEGTGQVIADPCPACAGQGVRQVRKKLRINIPAGVDTGTRLRVAGEGNAGLRGGPSGDLYVFLTVKSHPQLRRDGITVLSEVNVSYLQAILGDIIEVDTVDGNTSLEIPAGTQPNAVLTLENKGIPKLGNPVARGNQRISINVKLPIRLSDEERGLLEELAGHHSAKGRQHHHHNSGLFARLFGQKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.799 kDa
Sequence
MSKRDYYETLGVSQDASEKEVKKAYKKLAMKYHPDRTQGDKSKEETFKEVKEAYEILNDDQKRAAYDQYGHAAFEQGGNGGGGGGHGGGFGQDFGDIFGDIFGGGGGGRGRQRQQRGSDLRYNVDLSLEDAVKGKSLEIKVPTYVSCEPCDGSGAKKGTSAKTCSTCHGHGQVQMRQGLFAVQQTCPTCSGKGKVIADKCTSCRGQGRVEKTKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVNVRDHEIFVRDENHLYCEVPISFVTAALGGDIEVPTLGGKVKLKVPKETQTGKMFRLRGKGVKSVRSSTTGDLMCKVVIETPVNLSGDQADLLRQLEEKMASSSKKHSPKETGFFDGVKKFFDDLKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.186 kDa
Sequence
MAKQDYYESLGVAKSADEREIKKAYKRLAMKYHPDRNPGDSEAEAKFKEIKEAYEILIDSQKRAAYDQYGHAAFEQGGMGGSGGGFGGGGADFGDIFGDVFGDIFGGGRRQRASRGSDLRYNMELTLEEAVRGVTKEIRIPALEECDVCHGNGAKPGSSPITCPTCHGNGQVQMRQGFFTVQQACPHCHGRGKIIKDPCVKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPSGDLYVQVQVKAHPIFQREENNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPAETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVNLNERQRQLLQELDESFGGPSGERNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella sediminis (strain HAW-EB3)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.052 kDa
Sequence
MSKRDYYEVLSVSRDASEREIKKAYKRLAMKFHPDRNPGDKQAEANFKEVKEAYEILTDADKKAAYDQFGHAGVDPNRGGGGFGGNADFGDVFGDVFGDIFGGGRRGGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLAACDSCDGSGAKKGTSPTTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCNKCHGEGRVEKSKTLSVKIPAGVDNGDRIRLSGEGEAGEFGAPPGDLYVQVSVREHTIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVNLKIPAETQTGRMFRMRGKGVKSVRSHAVGDLLCKVVMETPVKLNERQKELLREFDETLTGSSSKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.933 kDa
Sequence
MSKRDYYEVLSVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAETSFKEVKEAYEILTDSDKKAAYDQFGHAGVDPNRGGGGFGGNADFGDVFGDVFGDIFGGGRRGGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLAHCDTCDGSGAKKGTSPTTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCNSCHGEGRVEKSKTLSVKIPAGVDNGDRIRLSGEGEAGEFGAPPGDLYVQVSVREHAIFVRDGNNLYCEVPISFGKAALGGEIEVPTLDGKVNLKIPAETQTGRMFRMRGKGVKSVRSHAVGDLLCKVVMETPVKLNERQKELLREFDETLAGSSSKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia cenocepacia (strain AU 1054)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.827 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia cenocepacia (strain MC0-3)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.827 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia cenocepacia (strain HI2424)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.827 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.827 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.841 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGGQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.866 kDa
Sequence
MAKRDYYEVLGVAKNAGDDEIKKAYRKLAMKYHPDRNPDNKDAEEHFKEVKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDNQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.87 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDNKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMAGAGGQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRMKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.916 kDa
Sequence
MAANRDYYDVLGVSRDASDAEISKAYRKLAKKYHPDLNHEAGAEEKYKEVNEAYEVLHDPQKRQQYDQFGQAGMNGQGGFGGQYGGQGFGGADFGDFGDIFSSFFGGARQQVDPTAPQRGADLDYTMTIDFMDAIKGKTSEISYSRSTTCEVCKGSGAEKGTHPITCDKCGGSGMMTITQRSVLGMIQRQTTCDKCTGSGVIIQHPCHNCHGKGVKTQKQTLQVKVPAGIDNGQQIRLAGQGEAGKNGGPYGDLYIVFRVRPSKDFTRRGQTIYTTVPISFAQATLGDEINVKTVYGDTKLKIPAGTQPNQKFTLKEKGVPSLRGGSTGDQVTTVEIVIPKSINEAQRKALLEFVKASGGSIAPQEKGFFERLKEKLS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.886 kDa
Sequence
MAANRDYYDVLGVSRDASDAEISKAYRKLAKKYHPDLNHEAGAEEKYKEVNEAYEVLHDPQKRQQYDQFGQAGMNGQGGFGGQYGGQGFGGADFGDFGDIFSSFFGGARQQVDPTAPQRGADLDYTMTIDFMDAIKGKTSEISYSRSTTCEVCKGSGAEKGTHPITCDKCGGSGMMTITQRSVLGMIQRQTTCDKCAGSGVIIQHPCHNCHGKGVKTQKQTLQVKVPAGIDNGQQIRLAGQGEAGKNGGPYGDLYIVFRVRPSKDFTRRGQTIYTTVPISFAQATLGDEINVKTVYGDTKLKIPAGTQPNQKFTLKEKGVPSLRGGSTGDQVTTVEIVIPKSINEAQRKALLEFVKASGGSIAPQEKGFFERLKEKLS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella oneidensis (strain MR-1)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.763 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEVKEAYEILTDANKKAAYDQFGHAGVDPNRGGGGGYGGAGDFGDIFGDVFGDIFGGGRRGGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLASCDVCDGSGAKKGTSATTCTTCHGQGQVQMRQGFFTVQQPCPTCHGRGKIIKDPCAKCHGDGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPAGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pyogenes serotype M1
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.494 kDa
Sequence
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYNLDISFTQAALGDTVEIPTVHGDVEMAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGEKMLHPKKKGFFDKVKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.494 kDa
Sequence
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYNLDISFTQAALGDTVEIPTVHGDVEMAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGEKMLHPKKKGFFDKVKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.453 kDa
Sequence
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYSLDISFTQAALGDTVEIPTVHGDVEMAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGDKMLHPKKKGFFDKVKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pyogenes serotype M18 (strain MGAS8232)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.453 kDa
Sequence
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYSLDISFTQAALGDTVEIPTVHGDVEMAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGDKMLHPKKKGFFDKVKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.502 kDa
Sequence
MNNTEFYDRLGVSKNASADEIKKAYRKLSKKYHPDINKEPGAEDKYKEVQEAYETLSDDQKRAAYDQYGAAGANGGFGGAGGFGGFNGAGGFGGFEDIFSSFFGGGGSSRNPNAPRQGDDLQYRVNLTFEEAIFGTEKEVKYHREAGCRTCNGSGAKPGTSPVTCGRCHGAGVINVDTQTPLGMMRRQVTCDVCHGRGKEIKYPCTTCHGTGHEKQAHSVHVKIPAGVETGQQIRLAGQGEAGFNGGPYGDLYVVVSVEASDKFEREGTTIFYNLNLNFVQAALGDTVDIPTVHGDVELVIPEGTQTGKKFRLRSKGAPSLRGGAVGDQYVTVNVVTPTGLNDRQKVALKEFAAAGDLKVNPKKKGFFDHIKDAFDGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pyogenes serotype M3 (strain SSI-1)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.494 kDa
Sequence
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYNLDISFTQAALGDTVEIPTVHGDVEMAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGEKMLHPKKKGFFDKVKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pyogenes
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.449 kDa
Sequence
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYSLDISFTQAALGDTVEIPTVHGDVELAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGEKMLHPKKKGFFDKVKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.161 kDa
Sequence
MSKKDYYEVLGLQKGASEQEIKRAYKRLAAKHHPDKNQGSKEAEEKFKEIKEAYEVLGDNEKRAMYDQYGHQAFEHGGGAGGFGGFGGGGFGGFEDIFSEMFGGGFGGGARRQRVVRGDDLRYDLEITLEEAVRGVKKDIRIRTLVQCDTCHGSGAEAGSKVETCPHCHGSGRVRRQQGFFMTETVCPSCHGTGKKIDKPCKSCHGDGRVEKTKNLSVTIPAGVDTGNQLRLSGEGAAGENGAPAGDLYVVIHVKDHDIFVRDGSNLYCEVPISFTMAALGGEIEVPTLDGRVKLKIPAETQTGKLFRVRGKGVTSARGGYAGDLICKVIIETPVSLNEEQKELLRKLEESLEGKGQHRPKHEGFFKGVKNFFDNLSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.469 kDa
Sequence
MAKKDYYQILGIPKSAEEREIKKAYKRLAMKYHPDRNQGDKNAENKFKEIKEAYEILINEEKRTAYDQYGHAAFENGYNQNNTYSTFTSSTDFGDIFGDVFGDIFGGSRNQRVKKGADLCYNMEISLEEAVKGTTKEIRIPTFQKCKTCYGMGTSTGTKPNGCSTCHGKGQIHIRKGFFTVQQSCPTCNGIGTVIKNPCRMCRGQGRIKTNKTLSVKIPPGIDTNDKIRLSKEGEAGTNGAQPGDLYVQMKVNKHPIFEREENNLYCEVPINFTMAALGGEIEVPTLDGRVNLKIPSETQSGKLFRIRGKGVKSVQSRSRGDLLCRVVVETPVNLNEKQKYLLSELGNSFNGFRGDKNSPRSKRFFDGVKRFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia ambifaria (strain MC40-6)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.841 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGGQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)
Length
378 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.672 kDa
Sequence
MAKRDYYEVLGVSKSASKDEIKKAYRKLSKQYHPDINKEEGADEKFKEISEAYEVLSDENKRANYDQFGHDGPQGGFGGQGFGGQDFSGFGGGGFEDIFSSFFGGGRQQRDPNAPRKGDDLQYTMTVTFDEAVFGSEKEISIRKDVACHTCDGEGAKPGTKKKTCHYCNGSGHVSVEQNTILGRVRTEKVCPVCSGSGQEFEEPCPTCHGKGTENKNVKISVTIPEGVDNEQQIRLAGEGAPGENGGPQGDLYIVFRVKPSEKFERDGDDIYYSLDISIAQATLGDEVKVPTLKGSVMLTIPAGTQTEKQFRLKEKGIKNVHGYGYGDLFININVVTPTKISDRQKELLREFAEIDGEELSEQPSNFRDKAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Synechococcus sp. (strain WH8102)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.053 kDa
Sequence
MADYYDLLGVGRDADADTLKRAYRSKARKYHPDINKEPGAEDRFKEIGRAYEVLSDPQTRARYDQFGEAGLGGAAGASDMGDMGGFADLFETFFQGFGGPGGAAAGRSGRRGPQQGDDLRYDLTIDFEQAVFGQEQEIKIPHLETCDTCGGSGAKAGSGPTTCGTCGGAGQVRRATRTPFGSFTQVAECPNCGGTGQVIADPCNACGGQGVRQVRKKLRINIPAGVDTGTRLRVSGEGNAGQRGGPSGDLYVFLTVKSHPRLRRDGLNILSTVNVSYLQAILGDTIEVETVDGDTVLEIPPGTQPGTVLTLANKGIPKLGNPVARGDQRVQVMVQLPTRLSDPERTLLEELAGHHSARGKQHHHHNSGLFARLFGQK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.877 kDa
Sequence
MAKRDYYEILGVAKNASEAELKKAFRRLAMKHHPDRNPGDKESEEKFKEAKEAYEILTDPQKRAAYDQFGHAGVDPSAGGGARGGASFSDIFEDIFGDIFGGGRGGGSRVYRGSDLQYNLELTLEEAVFGTEVKIRVPSLVECGECHGSGAEKGTTPETCGTCGGVGQVRMQQGFFSVQQTCPRCHGTGKMITHPCKACHGQGRVEEHKTLSVKVPAGVDSGDRIRLSGEGEAGINGGPPGDLYVQIHVKAHKLFTRKGNDLMCEVPISFATAALGGELEIPTLDGRVNLKIPEETQSGRLFRLRAKGVKSVHGGAQGDLICRVSVETPVNLTKRQKELLKELDETMKAGGTRHSPQEEGWLDGVKGFFEDLKFWNK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.806 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKFHPDRNPDSKDAEEKFKEAKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGAQGYGGFAEAFGDIFGDIFGQGGGGRRGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFTMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKPHAVFERDGDDLHCQMPISFATAALGGDLEVPTLSGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKEMLRQFDRSVHEGGSRHSPQETSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.232 kDa
Sequence
MKRDYYEVLGVSKSADEQEIKKAYRKLARQYHPDVNPGDKDAEEKFKEATEAYDVLSDTEKRARYDQMGHSAFDPNQQGFGGFGGDFGGFGDIFDMFFGGGGGGGQRRQGPTRGNDLRYDLTITFEEAAFGTEKEIQVPRQETCTECHGSGSAPGTHPTTCSQCHGTGQVKATQRTPFGAIQTARTCPACNGSGQFISSPCKECSGKGTTRKVKTIKVTVPPGSEDGLNLRFSGNGEAGLRGGPSGDLYVVLNVKAHKFFEREGNDVYCEIPITFVQAALGSELDVPTLDGKVKMKIPEGTQTATVFRLRGHGIPYRRGNGRGDQHVRVVVATPTKLTDRQKELLREFGEVTSDQQQMGKKSFFEKVKENIRDAIDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain PA7)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.23 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGGRGGARGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.26 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGARGGSRGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.26 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGARGGSRGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.26 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGARGGSRGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.806 kDa
Sequence
MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKFHPDRNPDSKDAEEKFKEAKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGAQGYGGFAEAFGDIFGDIFGQGGGGRRGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFTMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKPHAVFERDGDDLHCQMPISFATAALGGDLEVPTLSGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKEMLRQFDRSVHEGGSRHSPQETSWLDKVKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.232 kDa
Sequence
MKRDYYEVLGVSKSADEQEIKKAYRKLARQYHPDVNPGDKDAEEKFKEATEAYDVLSDTEKRARYDQMGHSAFDPNQQGFGGFGGDFGGFGDIFDMFFGGGGGGGQRRQGPTRGNDLRYDLTITFEEAAFGTEKEIQVPRQETCTECHGSGSAPGTHPTTCSQCHGTGQVKATQRTPFGAIQTARTCPACNGSGQFISSPCKECSGKGTTRKVKTIKVTVPPGSEDGLNLRFSGNGEAGLRGGPSGDLYVVLNVKAHKFFEREGNDVYCEIPITFVQAALGSELDVPTLDGKVKMKIPEGTQTATVFRLRGHGIPYRRGNGRGDQHVRVVVATPTKLTDRQKELLREFGEVTSDQQQMGKKSFFEKVKENIRDAIDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain PA7)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.23 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGGRGGARGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.26 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGARGGSRGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.26 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGARGGSRGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.26 kDa
Sequence
MAKRDFYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKEAEDKFKEANEAYEVLSDASKRAAYDQYGHAGVDPNMGGGAGAGFGGASFSDIFGDVFSDFFGGGGARGGSRGGAQRGADLRYTLDLDLEEAVRGTTVTIRVPTLVGCKTCNGSGAKPGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGTGKMISDPCGSCHGQGRVEEQKTLSVKVPAGVDTGDRIRLTGEGEAGSMGGPAGDLYVVVNVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPESTQTGKLFRLRGKGVAPVRGGGAGDLMCKVVVETPVNLDKRQRELLEEFRKSLQSDTSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.796 kDa
Sequence
MANKDYYELLGLQKGASDDEIKRAFRKLAVKYHPDRNQGNAEAEEKFKEINEAYQVLSDPEKKAKYDQFGSAAFDGSGGFGGGGFGGFDGFDMGGFGDIFESFFGGGGSNSRRRNGPVRGNDIEYTITLTFEEAVFGVEKEISVTRNENCEHCHGSGAEPGTNAKTCPTCSGSGQVRVQRQTPLGSFVSTSTCDTCRGTGKIIEKPCSECRGKGSVRKTRKIKVNIPAGVDTGNVMPLRGQGEHGLRGGSPGDLYVRINVTPSKVFTRKGNDVYIDAHISMPKAALGTEITVATVDGNVKYTVPPGTQSGTMFRLKGKGIQRVNSNGKGDQYVKVIVDIPKTLNKEQKEALYDFMRASGEEFDEANVPKKKLFGKNK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Orientia tsutsugamushi (strain Ikeda)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.492 kDa
Sequence
MSELDYYQVLGVSRTASQEEIKRAYRKLVLKYHPDHNPGDKNAEQKIKNINEAYDILKDEKKRSAYDQLGHQTFKNSGGGNYQQHHGFTGGIDPNDIFENIFGDFMGARRSSKTAFSKKAGANLKYDISLTLEEAFYGVTKIISFKTALTCEACTGKGSLDNNSTSSCPTCRGSGVTRSQQGFFFFENTCQTCRGAGHVIKNPCTKCYGEGRYINTRNLEVKIPAGVKEGSRIKLTGEGEAGSRGGKTGDLYVCITLIPHNTFSVDGNDLHCQLDINCTTAALGGEVEVTDITGSKLKLKIPAGTQNNHKLKLSGKGMQILHSDRCGNMIVHVNIKVPKSLTKSQRELMIKLDKELNEASEEGFLSKVRNFWTSGSE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.658 kDa
Sequence
MAKRDYYQVLGVAKNASDDEIKKAYRKLAMKHHPDRNPGNKDAEEHFKEAKEAYEMLSDSQKRAAYDQYGHAGVDPNMAGAGAQGFGGFADAFGDIFGDIFGQAAAGGRGGRSGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEICHGSGAKPGTKPETCPTCNGSGAVRMSQGFFSIQQTCPKCHGTGTYIPEPCTHCHGAGKTKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKAHAVFERDGDDLHCQMPIPFTKAALGGEIEVPTLAGRATFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDAQRDLLQQFEKSLVEGGARHSPQSKSWFDRVKSFFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfitobacterium hafniense (strain Y51)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.232 kDa
Sequence
MKRDYYEVLGVSKSADEQEIKKAYRKLARQYHPDVNPGDKDAEEKFKEATEAYDVLSDTEKRARYDQMGHSAFDPNQQGFGGFGGDFGGFGDIFDMFFGGGGGGGQRRQGPTRGNDLRYDLTITFEEAAFGTEKEIQVPRQETCTECHGSGSAPGTHPTTCSQCHGTGQVKATQRTPFGAIQTARTCPACNGSGQFISSPCKECSGKGTTRKVKTIKVTVPPGSEDGLNLRFSGNGEAGLRGGPSGDLYVVLNVKAHKFFEREGNDVYCEIPITFVQAALGSELDVPTLDGKVKMKIPEGTQTATVFRLRGHGIPYRRGNGRGDQHVRVVVATPTKLTDRQKELLREFGEVTSDQQQMGKKSFFEKVKENIRDAIDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma pulmonis (strain UAB CTIP)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.945 kDa
Sequence
MNKKEDYYKILGIDKSANEKEIKKAYRKLAMEHHPDRSSSKESEAKMREINEAYEVLSNPEKKAIYDKYGHEAANNPGFNGFNAGSAGFGNFGGFSNFGGFDSIFEEFFGGSRSHSKQNSNYPYPGESYSTQVKISFLDSVHGRVISQKLDKYKDCESCNGTGARSKSDIKTCSTCNGRGSVEKLVNSLFGKIKQSVTCSTCNGLGQEITHKCPSCKGAKKIKESISQKISIPAGVISGQEVLLRGFGGPGFNGGPNGDLYIRVYVTEHPYYQRINDDIYVDFPISIVNLILEKPVVVPTPYGDEKIKIKSTFKNDQIITFKGKGFKRKNRVGDLKIRLKFEIPNFSSKVKKNLESLLSETNDSINEDFVKKVNSIK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.101 kDa
Sequence
MKIDYYEALGVERTADDKVLKTAFRKLAMEYHPDRNPNNPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGSGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKAGSQPTTCTMCSGSGRVRAAQGFFSVERTCPTCNGRGQIIKDPCGKCHGQGRVTQERSLSVNIPAGIEDGTRIRLSGEGEAGMRGGPSGDLYIFLSVKPHEFFQRDGSDLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPDGTQNGKQFRLKGKGMPVLRQAAVGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Orientia tsutsugamushi (strain Boryong)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.344 kDa
Sequence
MSDLDYYQVLGVSRTASQEEIKRAYRKLVLKYHPDHNPGDKNAEQKIKNINEAYDILKDEKKRSAYDQLGHQAFKNSGGGNYQQHHGFTGGIDPNDIFENIFGDFMGARRSSKTAFSKKAGANLKYDISLTLEEAFYGVTKIISFKTALTCDACAGKGSLDNNSTSSCPTCRGSGVTRSQQGFFFFENTCQTCRGAGHVIKNPCTKCYGEGRYINTRNLEVKIPAGVKEGSRIKLTGEGEAGSRGGKTGDLYVCITLIPHNTFSVDGNDLHCQLDINCTTAALGGEVEVADITGSKLKLKIPAGTQNNHKLKLSGKGMQILHSDRCGNMIVHVNIKVPKSLTKSQRELMIKLDKELNEASEEGFLSKVRNFWASGSE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella sp. (strain ANA-3)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.704 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEVKEAYEILTDANKKAAYDQFGHAGVDPNRGGGGGYGGAGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLASCDVCDGSGAKKGSSATTCGTCHGQGQVQMRQGFFTVQQPCPTCHGRGKIIKDPCSKCHGDGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVTVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella sp. (strain MR-4)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.706 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEVKEAYEILTDANKKAAYDQFGHAGVDPNRGGGGGYGGAGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLASCDVCDGSGAKKGTSATTCGTCHGQGQVQMRQGFFTVQQACPTCHGRGKIIKDPCTKCHGDGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVTVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella sp. (strain MR-7)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.706 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEVKEAYEILTDANKKAAYDQFGHAGVDPNRGGGGGYGGAGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLASCDVCDGSGAKKGTSATTCGTCHGQGQVQMRQGFFTVQQACPTCHGRGKIIKDPCTKCHGDGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVTVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.083 kDa
Sequence
MAKQDYYEILGVERGADEKAIKKAYKRLAMKYHPDRTKGDKTSEEKFKEINEAYEILSDKEKRAAYDQYGHAAFEQGGFGGAGAGGFGGGFGGFGGFEDIFSEMFGGGSSRQRVVRGDDLRYDIEITLEEAVRGITKDIQIQTLATCDHCNGSGAEKGSKVETCPTCHGHGRVRRQQGFFMTETTCPHCHGTGKKIEKPCKKCHGDGRVHKTESLSVKIPAGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVKEHHIFERDGNNLYCEVPISFTQAALGGEIEVPTLDGRAKLKIPEGTQTGTMFRMRGKGITAMRSGYSGDLICKITVETPVKLTDEQKDLLHKLEASLEGKTTQRPKSSSFLDGVKKFFDNLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.894 kDa
Sequence
MAKADFYETLGVSKTADEKELKSAFRKLAMKFHPDKNPDDADSERKFKEINEAYETLKDPQKRAAYDRFGHAAFENGGMGGGGMGGGGFANGGFSDIFEDIFGEMMGGGRARRSSGGRERGADLRYNMEITLEEAFAGKTAQIRVPTSITCDVCSGSGAKPGTQPKTCATCQGSGRVRAAQGFFSVERTCPTCHGRGQTISDPCGKCHGQGRVTEERSLSVNIPSGIEDGTRIRLQGEGEAGMRGGPAGDLYIFLSVRPHEFFQRDGADLYCTVPISMTTAALGGTFDVTTLDGTKSRVTVPEGTQPGKQFRLKGKGMPVLRSAQTGDLYIQIQIETPQKLSKRQRELLQEFEQLSSKENNPESTGFFARMKEFFDG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.027 kDa
Sequence
MAKKDYYEVLGLQKGATEKDIKRAYKRLAAKYHPDKNQGSKDSEEKFKQITEAYEILTDDQKRAAYDQYGHAAFEQGSSNGGFNGFGGGFGGFEDIFSEMFGGGFGGGSRRQHVVRGQDLRYDIEISLEEAVKGCKKDIRLSTLAECDNCHGTGAEAGTKVENCPHCHGAGRIRRQQGFFVTEAVCPSCHGTGKKIEKPCHSCHGDGRVQKAKNLSVTIPAGVDTGNQLRLSGEGEAGENGAPAGDLYVVIHVREHNIFTRDGANLYCEVPISFSMAALGGEIEVPTLDGKLKLKIPTETQTGKLFRVRGKGVVSPRGGYAGDLICKVVVETPVQLNEEQKELLRQLEISLDGKANHRPQQAGFLDSVKNFFTHLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Klebsiella pneumoniae (strain 342)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.969 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGSKPQTCPTCHGAGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHAIFEREGNNLYCEVPINFTMAALGGEIEVPTLDGRVSLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLKELQESFGGPTGENNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.01 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGSKPQTCPTCHGAGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHAIFEREGNNLYCEVPINFTMAALGGEIEVPTLDGRVNLKIPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLKELQESFGGPTGENNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella baltica (strain OS223)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.865 kDa
Sequence
MSKRDYYEVLGVSRDTSEREIKKAYKRLAMKFHPDRNPGDKTAEANFKEIKEAYEILTDADKKAAYDQFGHAGVDPNRGGGGYGGGQGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLATCDLCEGSGAKKGTSATTCGTCHGQGQVQMRQGFFAVQQPCPTCHGRGKIIKDPCTKCHGDGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPAGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDRQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella baltica (strain OS155 / ATCC BAA-1091)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.865 kDa
Sequence
MSKRDYYEVLGVSRDTSEREIKKAYKRLAMKFHPDRNPGDKTAEANFKEIKEAYEILTDADKKAAYDQFGHAGVDPNRGGGGYGGGQGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLATCDLCEGSGAKKGTSATTCGTCHGQGQVQMRQGFFAVQQPCPTCHGRGKIIKDPCTKCHGDGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPAGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDRQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella baltica (strain OS185)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.865 kDa
Sequence
MSKRDYYEVLGVSRDTSEREIKKAYKRLAMKFHPDRNPGDKTAEANFKEIKEAYEILTDADKKAAYDQFGHAGVDPNRGGGGYGGGQGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLATCDLCEGSGAKKGTSATTCGTCHGQGQVQMRQGFFAVQQPCPTCHGRGKIIKDPCTKCHGDGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPAGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDRQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella baltica (strain OS195)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.877 kDa
Sequence
MSKRDYYEVLGVSRDTSEREIKKAYKRLAMKFHPDRNPGDKTAEANFKEIKEAYEILTDADKKAAYDQFGHAGVDPNRGGGGYGGGQGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLATCDLCEGSGAKKGTSATTCGTCHGQGQVQMRQGFFAVQQPCPTCHGRGKIIKDPCSKCHGDGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDRQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.498 kDa
Sequence
MSKRDYYEVLGVGRDSSERDIKKAYKRLAMKFHPDRNPGDKAAEASFKEIKEAYEILTDGDKKAAYDQFGHAGVDPNRGGGGHGGGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVRGLTKELRIPTLAACDLCDGSGAKKGTSASSCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCGKCYGEGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPAGDLYVQVSVREHGIFTRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPTETQTGRMFRLRGKGVKSVRSHAIGDLLCKVVMETPVNLSEQQKELLREFEASLTGAGASKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.858 kDa
Sequence
MNNQEYYDRLGVSKDASQDEIKKAYRRMSKKYHPDINKEPGAEEKYKEIQEAYDTLGDEQKRAAYDQYGPAGANGGFGDGSGFSGFDSSGFGGFEDIFSSFFGGGASRNPNAPRQGDDLQYRVNLQFEEAVFGTEKEVHYNREASCHTCNGSGAKPGTSPVTCSKCHGSGVINMDTQTPLGMMRRQVTCDVCHGTGQEIKEPCPTCHGTGHEKQSHKVSVKIPAGVETGQQIRLAGQGEAGFNGGPYGDLFVIINVLKSDKFERDGSTIYYSMDINFVQAALGDTVEVPTVHGNVELAIPAGTQTGKTFRLKGKGAPRLRGNGQGDQHVTVNVVTPTKLNDAQKEALQDFAKASGINPVHPKKKGFFNKVKDAFDEM

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus thermophilus (strain CNRZ 1066)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.585 kDa
Sequence
MNNTEYYDRLGLSKDASQDEIKRAYRKLSKKYHPDINKEPGAEEKYKEILEAYETLSDAQKRAAYDQYGPDGANGFGGQGSFGGFDGGAGFGGFEDIFSSFFGGGATRNPNAPRQGDDLQYRVNLSFEEAVFGAEKEIHYNREVTCKTCSGSGAKPGTSPVTCGRCHGHGVINVDTQTPLGMMRRQVTCDVCHGTGQEIKDPCQTCHGTGREKQSHTVSVKIPAGVETGQQIRLAGQGEAGFNGGPYGDLFVVINVNPSDKFTRDGSTIYYTLNISFVQAALGDTVEVPTVHGNVEMVIPAGTQTGKTFRLKGKGAPRLRGGSQGDQLVTVKIVTPTKLNDAQKEALLAFAKASGDEKVAPQKKGFFNKVKDVLEDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.585 kDa
Sequence
MNNTEYYDRLGLSKDASQDEIKRAYRKLSKKYHPDINKEPGAEEKYKEILEAYETLSDAQKRAAYDQYGPDGANGFGGQGSFGGFDGGAGFGGFEDIFSSFFGGGATRNPNAPRQGDDLQYRVNLSFEEAVFGAEKEIHYNREVTCKTCSGSGAKPGTSPVTCGRCHGHGVINVDTQTPLGMMRRQVTCDVCHGTGQEIKDPCQTCHGTGREKQSHTVSVKIPAGVETGQQIRLAGQGEAGFNGGPYGDLFVVINVNPSDKFTRDGSTIYYTLNISFVQAALGDTVEVPTVHGNVEMVIPAGTQTGKTFRLKGKGAPRLRGGSQGDQLVTVKIVTPTKLNDAQKEALLAFAKASGDEKVAPQKKGFFNKVKDVLEDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus uberis (strain ATCC BAA-854 / 0140J)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.513 kDa
Sequence
MNNTEFYDRLGVSKDASQDEIKKAYRKMSKKYHPDINKEPGAEQKYKDVQEAYETLSDAQKRSAYDQYGAAGAQGGFGGGGFGGFDGGGFGGFEDIFSSFFGGGGGMRNPNAPRQGDDLQYRVNLTFEEAIFGVEKDVSYHREATCHTCAGSGAKPGTSPVTCGRCHGSGVINVDTQTPLGMMRRQVTCDVCHGSGKEIKEPCQTCHGTGHEKETHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVVLNVLPSQKFERNGSTIYYNLNISFVQAALGDTVDIPTVHGDVEMAIPAGTQTGKVFRLKGKGAPKLRGAGQGDQHVTVNIVTPTKLNEKQKEALRAFAEASGQEISTPKKKGFFDKMKDALEDI

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Sulfurovum sp. (strain NBC37-1)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.287 kDa
Sequence
MSEMDYYEVLEVSRDCSGAELKKAYRKLALKYHPDRNPDDQEAEEKFKIVNEAYQVLSDDEKRTIYDRYGKEGLEGQGMGGGFGGANMDDIMDIFNSMFGGGGGGFGGFGRTRRDPSQKYALDFEIELPLAFNEAVFGCEKKIDITYKTPCEECGGTGAKDGKMETCDYCGGQGQVLMRQGPMQFAQTCPKCHGEGRKIAQKCPSCQGKGYHEETETVTIKVPAGVDSGNRLRVPGHGNEAKNGQRGDLYLTFYVEEDEHFIRNGNDIYIEVPVFFTQAILGETISIPTLDGELELELKQSTKDKEQFIFEGEGVPDVHNGRKGRLIAQVRMILPKKINEEQKELLEKLQESYGVESRPHKSTFESAFDKVKNWFKN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus pumilus (strain SAFR-032)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.023 kDa
Sequence
MSKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEAGSDEKFKEVKEAYETLSDDQKRSQYDQFGHTDPNQGFGGGGFGGGGDFGGFGGFDDIFSSIFGGGARRRDPNAPRQGADLQYTMTLSFEEAAFGKEATIEIPREESCETCHGSGAKPGTDAKTCSHCGGSGQLNVEQSTPFGKVVNRRVCNYCSGTGKQIDHKCSTCGGSGKVRKRKKINVTIPAGVDDGQQLRVSGQGEPGVNGGPPGDLFVVFHVRSHEFFERDGDDIYCEMPLTFAQAALGDEIEVPTLHGKVKLKVPAGTQTGTKFRLKGKGVKNVRGYGQGDQHIVVRVVTPTNLTDNQKDIIRKFAEVSGNKPDEQEMSFFDKVKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Blochmannia floridanus
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.379 kDa
Sequence
MVKSDYYEILGVSKNADEREIKKSYKRLAMKFHPDRNPGDVSAESKFKEIKEAYEVLSNPEKRSAYDQYGHAIFEQNSGGMGGSNTGGSDFSDIFGDVFGDIFGGSRRSRSRRGSDLRYDIELSLEEAVKGVVREICVPTLVTCLQCRGSGAKSSASIVSCVTCHGHGQIQMRQGFFSVQQSCPSCNGHGKIIKEICNKCRGSGRIERTKTLSVKIPAGVSTGDRIRLSGEGESGKNGAPAGDLYVQVQIKKHPIFDREEKNLYCEVPISFSMAALGGEIEVPTLDGRVKLKIPPETQTGKLFRMRGKGVKSVRGIGGHGDLLCRVVVETPVRLSDRQKQLLQDLSDSFGGPYGHKNSPKSKTFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.551 kDa
Sequence
MAKRDYYEVLGVAKNASDEDLKKAYRKLAMKYHPDRNPDSKEAEEKFKEAKEAYEVLGDEQKRAAYDRYGHAGVDPNAAGMGGGMGGGMGGGFADAFGDIFGEIFGAGRRGGGGPQVYRGADLKYALEITLEQAASGFDTEIRVPSWENCDTCHGSGAKAGTSPKTCRTCGGSGAVRMQQGFFSVQQTCPTCHGTGKEITDPCPSCDGVGRTRRNKTLQVKIPAGIDDGMRIRSSGNGEPGINGGPPGDLYVEIHIKQHKIFQRDGDDLHCELTIPFTTAALGGELQVPTLGGKAEISIPEGTQSGKTFRLRAKGIRGVRGSYPGDLYCHVVVETPVRLSDEQKAILRQFEASLNDGGDRHSPQSKSWTDRVKEFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.945 kDa
Sequence
MSTSTKRCYYETLEVERDADESKLKSSFRKLAMKFHPDRNPGDDTSEVKFKEINEAYEVLKDKDKRAAYDRFGHAAFEQGGPGGGAGFGAGFASSFSDIFEDLFGMAGQRGRGGRERGADLRYNMEITLEEAFGGKTAQIEIPVSVTCEACSGIGAKAGTKPKTCSTCGGAGRVRQSQGFFTLERTCPGCQGRGQMIEDACPSCSGQGRVTRERTLSVNIPQGVEDGTRIRLAGEGEAGVRGGPPGDLYIFLSLAQHQFFQRDGADLHCRVPISMVTAALGGEFEVPTIEKGKAKVKVPAGTQSNRRFRIASKGMPVLRSRQTGDMYVQVVVETPQNLTKKQQELLAEFEKLSSGNTQPESEGFFTKVKDFFGSRAN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella abortus (strain S19)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.108 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPTGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella abortus (strain 2308)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.108 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPTGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella abortus biovar 1 (strain 9-941)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.108 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPTGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella canis (strain ATCC 23365 / NCTC 10854)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.078 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.078 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.078 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.143 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSWQENSPKSAGLFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella suis (strain ATCC 23445 / NCTC 10510)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.078 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brucella suis biovar 1 (strain 1330)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.078 kDa
Sequence
MKIDYYEALGVTRTADDKTLKAAFRKLAMQYHPDRNPDDPEAERKFKEIGEAYETLKDPQKRAAYDRFGHAAFENGGMGGGFGNGFGGAGGFADIFEDIFGEMMGGGRRRSNGGRERGADLRYNMEVTLEEAYAGKTAQIRVPTSITCDECSGSGAKPGSQPTTCTMCSGSGRVRAAQGFFSVERTCPGCNGRGQIIKDPCEKCHGQGRVTQERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPAGDLYIFLSVKPHEFFQRDGADLYCKVPISMTTAALGGQFEVSTLDGTQTRVKVPEGTQNGKQFRLKGKGMPVLRQSVTGDLYIQIDIETPQNLSKRQRELLEEFEKLSSQENSPKSAGFFSRMKEFFEGIGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.344 kDa
Sequence
MAKKDYYQILGIPKSAEEREIKKAYKKLAMKYHPDRNQGDKTAEGKFKEIKEAYEILINEEKRSAYDQYGHAAFENGQSNSTYSTFTNSADFSDIFGDVFGDIFGGNRTQRAKKGADLCYNMEITLEEAVKGIKKEIQIPTLQKCKTCYGSGTRTGTKPRSCSTCHGKGQIHIRKGFFTVQQSCPTCHGKGTIITDPCNLCHGQGRVETYKILSVKIPPGLDTNDRIRLNNEGEAGANGAQSGDLYVQITVKKHPIFEREGNNLYCEVPINFTMAALGGEIEVPTLDGRVKLKIPYETQSGKLFRIRGRGVKSVQNRNQGDLLCRVVVETPVNLNEQQKNLLHELGNSFHGFRGEKNSPRSKRFFDGVKRFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.344 kDa
Sequence
MAKKDYYQILGIPKSAEEREIKKAYKKLAMKYHPDRNQGDKTAEGKFKEIKEAYEILINEEKRSAYDQYGHAAFENGQSNSTYSTFTNSADFSDIFGDVFGDIFGGNRTQRAKKGADLCYNMEITLEEAVKGIKKEIQIPTLQKCKTCYGSGTRTGTKPRSCSTCHGKGQIHIRKGFFTVQQSCPTCHGKGTIITDPCNLCHGQGRVETYKILSVKIPPGLDTNDRIRLNNEGEAGANGAQSGDLYVQITVKKHPIFEREGNNLYCEVPINFTMAALGGEIEVPTLDGRVKLKIPYETQSGKLFRIRGRGVKSVQNRNQGDLLCRVVVETPVNLNEQQKNLLHELGNSFHGFRGEKNSPRSKRFFDGVKRFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.314 kDa
Sequence
MAKKDYYQILGIPKSAEEREIKKAYKKLAMKYHPDRNQGDKTAEGKFKEIKEAYEILINEEKRSAYDQYGHAAFENGQSNSTYSTFTNSADFSDIFGDVFGDIFGGNRTQRAKKGADLCYNMEITLEEAVKGIKKEIQIPTLQKCKTCYGSGTRTGTKPRSCSTCHGKGQIHIRKGFFTVQQSCPTCHGKGTIIADPCNLCHGQGRVETYKILSVKIPPGLDTNDRIRLNNEGEAGANGAQSGDLYVQITVKKHPIFEREGNNLYCEVPINFTMAALGGEIEVPTLDGRVKLKIPYETQSGKLFRIRGRGVKSVQNRNQGDLLCRVVVETPVNLNEQQKNLLHELGNSFHGFRGEKNSPRSKRFFDGVKRFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria monocytogenes serotype 1/2a (strain 10403S)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.077 kDa
Sequence
MAKRDYYEVLGISKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGGAGGGFGGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.077 kDa
Sequence
MAKRDYYEVLGISKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGGAGGGFGGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.638 kDa
Sequence
MAKEDYYETLGVPRNASDSDIKKAFRRLAMKYHPDRNKDNPEAEERFKSVKEAYDVLSDPKKRSAYDQFGHAGIDPSMGGGGGFGFTGDSFSDIFGDVFGDIFGGGGRRRGRGQRGSDLRYNLELTLEEAVAGTEAKIKVPTWVTCTECGGSGAKKGSAPVTCPTCHGQGAVRMQQGFFSVQQTCPTCRGTGQHISDPCRVCYGQGRVQETKTLSVKIPPGVDTGDRIRLSGEGEAGEGGGPPGDLYVHIGVKQHPIFTRDGADLYCEVPIGFPTACLGGELEVPTLDGKVVLKIPAETQTGRLFRVRGKGVKPVRGGVAGDLLCRVRVETPVHLNKEQIDLIRQLDESLRGGGSHHSPQAHGWLDGVKQFFDRLGL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus carnosus (strain TM300)
Length
377 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.59 kDa
Sequence
MAKRDYYEVLGVSKDASKDEIKKAYRKLSKKYHPDINQEEGAEEKFKEISEAYEVLSDENKRANYDQFGHDGPQGGFGGQGFGGGQDFGGFGGGFEDIFSSFFGGGAQRDPNVPRKGDDLQYTMTVTFEEAAFGTEKEISIRKQVKCETCDGSGAKPGSKKKTCHYCNGSGHVSVEQNTILGRVRTEKVCPVCNGTGEEIEEPCPTCHGKGTETKNVKIKVKVPEGVDNDQQIRLAGEGAPGHNGGPQGDLYVVFRVEPSDTFEREGDDIFYNLNVSFPQAALGDEIKVPTLKGHVMLSVPEGTQNGKQFRMKEKGIKNVHGYGYGDLFININVVTPTKLNDKQKSIMREFAEVSGEEITEQPTNFKERARRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MAADYYQLLGVARDADKDEIKRAYRRLARKYHPDVNKEPGAEDKFKEINRAYEVLSEPETRARYDQFGEAGVSGAGAAGFQDFGDMGGFADIFETFFSGFGGMGGQQASARRRGPTRGEDLRLDLKLDFRDAIFGGEKEIRVTHEETCGTCQGSGAKAGTRPQTCTTCGGAGQVRRATRTPFGSFTQVSVCPTCEGSGQMIVDKCDDCGGAGRLRRPKKLKINIPAGVDSGTRLRVANEGDAGLRGGPPGDLYVYLFVSEDTQFRREGINLFSTVTISYLQAILGCSLEVATVDGPTELIIPPGTQPNAVLTVEGKGVPRLGNPVARGNLLVTIKVEIPTKISAEERELLEKVVQIRGDRAGKGGIEGFFKGVFGG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Teredinibacter turnerae (strain ATCC 39867 / T7901)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.332 kDa
Sequence
MAKRDYYEVLGVARDVSEQDLKKAYRKVAMKFHPDRNPDDASAEEKFKEASEAYEVLSDKQKRAAYDQFGHAGVEGQGGMGGGAEGFGSFSDIFGDVFGDIFGGAGGGRGRGGPSRGADLRYTLDLSLEDAVRGTSVKIKVPTLVSCTNCGGSGAKPGTTATTCNTCGGHGQVRMQQGFFSVQQTCPTCRGQGKTISDPCNKCHGHGRVEETKTLSVKVPAGVDTGDRIRLAGEGEAGADGGPSGDLYVQVHVKDHEFFQREGRNLYCEVPISIFDACLGGDLEVPTLDGRVKLKVPAETQTGKLFRLRGKGVTPIRGGAAGDLLCRVIVETPVNLSNKQKELLEQLKDTFKGTQHSPKQQSWFEGMKNFFGDMKM

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Tolumonas auensis (strain DSM 9187 / TA4)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.855 kDa
Sequence
MAKRDYYEILGVERSADEREIKKAYKRLAMKFHPDRNPDNPESEEKFKEAKEAYEILSDAQKRAAYDKFGHAGVDPNQAGPGGFGGGADFGDVFGDIFGDIFGGGRRSQRAARGSDLRYNMELTLEEAVRGVSKEIKVPTLVECDECHGSGARTGTSAQTCPTCHGSGQVQMRQGFFAVTQACPHCHGKGKIITDPCRKCHGDGRVQKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPAGDLYVQVHVKEHPIFVRDGNNLYCEIPISFTTAALGGEVAVPTLDGRVMLKIPVETQTGRMFRLRGKGVRSLRSGAEGDLLCKAVVETPVKLSDEQKELLKQLEDSLNGSGVKTHKPKADGFFEGVKRFFDDLTG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain ATCC 51142)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.798 kDa
Sequence
MPGDYYDILGVDRNASKEDLKRAYRRLARKYHPDVNKEPGAEERFKEINRAYEVLSEPDTRSRYDQFGEAGVSGAGGFNYGDMGDMGGFADIFETIFSGFGGGMGTGGTRRRTGPVKGDDLRLDLKLDFREAVFGGEKEIRIPHLETCQVCKGDGAKPGTGAKTCSTCNGQGQVRRATRTPFGSFAQVSACPACNGQGQVIEEKCEVCNGAGRRQVTEKVKITIPAGVDDGTRLRVSRKGDAGLRGGPQGDLYVYLYVEPDKVFTRDKMNILSEITISYLQAILGCTVTVDTVDGEQELTIPAGTQPNTILTLENLGVPKLGNDAIRGDHLITVKVDIPTRINAEERELLEKLAHIKGQSHGKGGLEGFLGSLFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.238 kDa
Sequence
MDYYELLGVSRTASADEIKSAYRKLALKLHPDRNKEEGAAEKFAQVSEAYSVLSDTEKRAHYDRFGSAPGAGMPGGDXFGGMGGMGGVGFDPMDIFEQLFGGAAGMGGRGRRGPARGDDLETEVRITLEQARAGEEVEVTVDRLTECEHCHGTRTEPGGKPPVTCSTCNGSGAVRGQARTIFGVVETQQVCPTCKGDGKMVVDPCTVCHGRGRTLKSEPVKVKLPKGIDEGYRIRVAGQGNEGPGGNGDLYVHIEMEPHPELHRQDENLIFPARIGFATAALGGRIQVPTLDGPQEVEVKPGTQHGELHRLRGQGMPRLQGAGTGDLIVDYEIVVPKHLNAEAKDALQAYARAVGDEVPEEHEGLFGKIGKLFGRD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain ATCC 51142)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.798 kDa
Sequence
MPGDYYDILGVDRNASKEDLKRAYRRLARKYHPDVNKEPGAEERFKEINRAYEVLSEPDTRSRYDQFGEAGVSGAGGFNYGDMGDMGGFADIFETIFSGFGGGMGTGGTRRRTGPVKGDDLRLDLKLDFREAVFGGEKEIRIPHLETCQVCKGDGAKPGTGAKTCSTCNGQGQVRRATRTPFGSFAQVSACPACNGQGQVIEEKCEVCNGAGRRQVTEKVKITIPAGVDDGTRLRVSRKGDAGLRGGPQGDLYVYLYVEPDKVFTRDKMNILSEITISYLQAILGCTVTVDTVDGEQELTIPAGTQPNTILTLENLGVPKLGNDAIRGDHLITVKVDIPTRINAEERELLEKLAHIKGQSHGKGGLEGFLGSLFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.238 kDa
Sequence
MDYYELLGVSRTASADEIKSAYRKLALKLHPDRNKEEGAAEKFAQVSEAYSVLSDTEKRAHYDRFGSAPGAGMPGGDXFGGMGGMGGVGFDPMDIFEQLFGGAAGMGGRGRRGPARGDDLETEVRITLEQARAGEEVEVTVDRLTECEHCHGTRTEPGGKPPVTCSTCNGSGAVRGQARTIFGVVETQQVCPTCKGDGKMVVDPCTVCHGRGRTLKSEPVKVKLPKGIDEGYRIRVAGQGNEGPGGNGDLYVHIEMEPHPELHRQDENLIFPARIGFATAALGGRIQVPTLDGPQEVEVKPGTQHGELHRLRGQGMPRLQGAGTGDLIVDYEIVVPKHLNAEAKDALQAYARAVGDEVPEEHEGLFGKIGKLFGRD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium novyi (strain NT)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.383 kDa
Sequence
MASKDYYEVLGLSKGASDDEIKKAYRKLAMKYHPDRNQGNKEAEEKFKDINEAYQVLSDPQKKANYDQFGSADFNGGGFGGFGGGGFSGMGGFEDIFDSFFGGGFSSRRRNGPERGADLEYTVSLTFEEAVFGVEKEISITRNEKCDTCAGSGAKPGTDSKTCDKCGGTGQVRVQRNTPLGSFVSTSTCDKCGGSGKVIDEPCTTCHGKGTVRKNKKIKINIPAGVDTGNVLPLRGQGEPGKNGGPNGDLYINIRVSSHKNFERRGFDIYIKEHISFGKAVLGTEITVPTVDGSVKYKIPAGTQSGTTFRLKGKGVPRVNGHGRGNQYVKVIVDVPKAINEKQKAALIAFMEASGEKLGSDLGKETIVDKIKKSFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pelagibacter ubique (strain HTCC1062)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.827 kDa
Sequence
MAKRDFYDVLGVSKSASPEELKSAYRKLAVKYHPDKNPGDKASEDKFKEAGEAYGVLSDKEKKQNYDNFGHAAFEGGGGRQGGGFGGGFGGADFSDIFEDFFGDFGGGQSRGRRKTNNRGSDLRYDLSITLEEAYEGKKQDIKFSTTEKCNTCNGNGSKPGHSPDRCTVCGGNGKVRSNQGFFTVQQTCPQCAGSGEEITNPCTDCNGQGNKQASKKISVTIPKGVDDGTRIRLAGKGEAGSKGGANGDLYLFVNVHSHDLFKRSDENLFFEFPISIADAALGTTIEIPTIDGGKAKIKIPDGTQNGKQFRLKGKGMPYMRGSGNGDLYVQVNTEVPISLNKEQKALLEKFREIENEKSNPSIKQFFQKAKSFWKN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas campestris pv. campestris (strain 8004)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.53 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKYHPDRNPGDAAAEATFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECEPCHGSGSEDGKVEVCATCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTTDQRELLKQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.5 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKYHPDRNPGDAAAEATFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECEPCHGSGSEDGKVEVCATCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLKQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.53 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKYHPDRNPGDAAAEATFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECEPCHGSGSEDGKVEVCATCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTTDQRELLKQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.42 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKHHPDRNPGDAAAEAAFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGSPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECVSCHGSGSEDGKVQTCGTCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEENKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLQQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas oryzae pv. oryzae (strain PXO99A)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.42 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKHHPDRNPGDAAAEAAFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGSPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECVSCHGSGSEDGKVQTCGTCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEENKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLQQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.42 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKHHPDRNPGDAAAEAAFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGSPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECVSCHGSGSEDGKVQTCGTCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEENKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLQQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.975 kDa
Sequence
MAKRDYYEVLGVKKDADEREIKKAYKRLAVKYHPDRNQDENDTGENFKEVKEAYEILTDPQKRAAYDQYGHAAFEQGGMGGGGFGGGGADFTDIFGDVFGDIFGGGRRQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLNECDVCHGSGAKPGSSPVTCSTCRGAGQVHMRQGFFTVQQACPTCHGSGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPAETQTGKLFRMRGKGVKSVRGGSQGDLLCRVVVETPVHLSEKQKQLLRELEESFVGAAGEKNSPRSKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.929 kDa
Sequence
MSQRDYYEVLGVARDASEDDIKRAYRKLALQYHPDRNPDDPEAEQKFKEAAEAYDVLRDGEKRARYDRFGHAGVGNGGGFGQGFSSNEDIFAHFSDIFGDLFGFAGAAGGRSRGPRPQAGSDLRYNLTISFRQAAKGDEVTLRLPKSVPCDECGGSGAAPGTRPETCRHCGGAGQIRQSQGFFQIAMPCPVCRGEGTVITSPCPKCKGSGQTQQVKELSVRIPAGVDTGNRLRLRGEGEPGIHGGPAGDLYVVISVEDDKTFRRQGQDLVVTREISFVQASLGDRIDVPTLDDDITLDIPAGTQSGEVFRLVDKGLPYLGHGHTGDLLVEIRVVTPTRLTKKQEELLREFALLDEEKPLEKVKKMARKIGKAMGMD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio vulgaris subsp. vulgaris (strain DP4)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.929 kDa
Sequence
MSQRDYYEVLGVARDASEDDIKRAYRKLALQYHPDRNPDDPEAEQKFKEAAEAYDVLRDGEKRARYDRFGHAGVGNGGGFGQGFSSNEDIFAHFSDIFGDLFGFAGAAGGRSRGPRPQAGSDLRYNLTISFRQAAKGDEVTLRLPKSVPCDECGGSGAAPGTRPETCRHCGGAGQIRQSQGFFQIAMPCPVCRGEGTVITSPCPKCKGSGQTQQVKELSVRIPAGVDTGNRLRLRGEGEPGIHGGPAGDLYVVISVEDDKTFRRQGQDLVVTREISFVQASLGDRIDVPTLDDDITLDIPAGTQSGEVFRLVDKGLPYLGHGHTGDLLVEIRVVTPTRLTKKQEELLREFALLDEEKPLEKVKKMARKIGKAMGMD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli (strain 55989 / EAEC)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O157:H7
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.074 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAETKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O81 (strain ED1a)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O8 (strain IAI1)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.128 kDa
Sequence
MVKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNERQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli (strain K12 / DH10B)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.1 kDa
Sequence
MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNERQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Escherichia coli O9:H4 (strain HS)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.073 kDa
Sequence
MARDYYEILGVARDADKEEIKQAYRRLARKYHPDVNKEPGAEERFKEINRAYEVLSEPETRARYDRFGPEGVSGAGVGFQDMSDMGGFADIFESIFSGFAGGGMGGPTQQRRRGGPARGDDLRLDLKLDFREAVFGGEKEIRISHLETCETCSGSGAKPGTRPRTCSTCSGSGQVRRVTRTPFGSFTQVSTCPTCNGTGMVIEDKCDTCDGKGTNQVTKKLKITIPAGVDNGTRLRIKDEGDAGQRGGPPGDLYVYLFVNEDEEFQRDGINVISEIKVSYLQAILGCRLEVNTVDGPVELIIPAGTQPNTVMKLENRGVPRLGNPVSRGDHLLTVLIDIPTKVIPEERELLEKLAKIKGDRTGKGGLEGFLGNLFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.751 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEAKEAYEILTDTDKKAAYDQFGHAGVDPNRGGGYGGGQGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLATCDLCDGSGAKKGTSASTCTTCHGQGQVQMRQGFFTVQQPCPTCHGRGKIIKDPCTKCHGDGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDRQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella piezotolerans (strain WP3 / JCM 13877)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.863 kDa
Sequence
MSKRDFYEVLGVGRDASEREVKKAYKRLAMKFHPDRNPGDKEAEASFKEVKEAYEILTDSDKKAAYDQFGHAGVDPNRGGGGHGGADFGDVFGDVFGDIFGGGRRGGGQRQAARGSDLRYNLELSLEEAVKGLSKELRIPTLVACEPCDGSGAKKGSKPTTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCNKCHGEGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEFGAPPGDLYVQVSVREHAIFQRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVNLKIPTETQTGRMFRMRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEETLTGQSKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella sp. (strain W3-18-1)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.737 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEAKEAYEILTDTDKKAAYDQFGHAGVDPNRGGGYGGGQGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVKGLTKELRIPTLATCDLCDGSGAKKGTSASTCTTCHGQGQVQMRQGFFTVQQPCPTCHGRGKIIKDPCSKCHGDGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVSVREHAIFVRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDRQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.043 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGQHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shigella boydii serotype 4 (strain Sb227)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.043 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGQHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.072 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEVGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.072 kDa
Sequence
MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shigella flexneri
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.139 kDa
Sequence
MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETQIGLDEKDKQLLHELHESYGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shigella sonnei (strain Ss046)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Acidovorax sp. (strain JS42)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.838 kDa
Sequence
MSKRDFYEVLGVPKNASDDEIKKAYRKLAMKYHPDRNQGDAAKPAEEKFKEAKEAYEILSDAQKRAAYDQYGHAGVDPNMRGGMGGAEGFGGFAEAFGDIFGDMFGGARGRGGRQVYRGNDLSYAMEITLEEAAKGKEAQIRIPSWESCETCHGSGAKPGTSAKTCGTCQGSGTVQMRQGFFSVQQTCPHCRGTGKIIPEPCTACHGQGRVKKQKTLEVKIPAGIDDGMRIRSTGNGEPGTNGGPPGDLYIEIRIKKHDIFERDGDDLHCQVPVSFITAALGGEIEVPTLQGKAAIDIPEGTQAGKQFRLRGKGIKGVRSSYPGDLYCHIIVETPVKLTEHQRKLLKELDESLKKGGAKHSPSTESWTDRLKSFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.142 kDa
Sequence
MSKRDYYEVLGAAKDASAQDLKKAYRRLAMKYHPDRNPDDKEALAKFKEAKEAYEVLADEQKRAAYDQFGHAGVNGQGGGPGAGAGAGGFGDIFGDIFGDIFGGAGGGGGRRGPSRGADLRYTLELSLEQAVRGCDEKIRIPTWDSCDVCHGSGAKEGSQPVTCTTCGGVGQVRMQQGFFTVQQACPTCKGEGKIIKDPCGNCGGQGRVQNTKTLSVKIPAGVDTGDRIRLAGEGEAGVHGAPSGDLYVQVAVREHDIFQRDGDNLYCEVPISFVDATLGGELDVPTLNGKVKLKVPAETQSGKLFRLRGKGVAPVRGGAPGDLLCKVVIETPVKLSSEQKELLRKFQESLESGGNRHNPRKNNWFEGVKRFFDTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.056 kDa
Sequence
MARDYYEILGVARDADKEEIKQAYRRLARKYHPDVNKEPGAEERFKEINRAYEVLSEPETRARYDRFGPEGVSGAGVGFQDMSDMGGFADIFESIFSGFAGGGMGGPTQQRRRGGPARGDDLRLDLKLDFREAVFGGEKEIRISHLETCETCSGSGAKPGTRPRTCSTCSGSGQVRRVTRTPFGSFTQVSTCPTCNGTGMVIEDKCDACDGKGTNQVTKKLKITIPAGVDNGTRLRIQQEGDAGQRGGPPGDLYVYLFVNEDEEFQRDGINVISEIKVSYLQAILGCRLEVNTVDGPVELIIPAGTQPNTVMKLENRGVPRLGNPVSRGDHLLTVLIDIPTKVIPEERELLEKLAKIKGDRTGKGGLEGFLGNLFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia bellii (strain OSU 85-389)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.878 kDa
Sequence
MSQDYYQILGVSKTANSADLKKAYHKLAKQYHPDNAAAGDTNAEKKFKEINAAYEVLKDEQKRAAYDRFGHDAFQNQQARGGAGSQGGHPFGADINDIFGDFFSDFMGGGGRRKPTSSKVRGSDLKYNLTINLEEAFHGVEKNISFSSEVKCDTCHGSGSEKGETTTTCDACGGVGATRVQQGFFMIEQTCHKCQGNGQIIKNPCKKCHGLGRYHKQRNLSVNIPAGVENGTRIRHPGEGEAGIRGGNNGDLYVDIAIKPHDIYKVDGANLHCKLPISFVNAALGGEVAVPVIEGGKVNLTIPAGTQNGDQLRLCGKGMSKIRSTIRGDMLAHVHVEVPKNLSKRQRELLEELRGESANEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia bellii (strain RML369-C)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.894 kDa
Sequence
MSQDYYQILGVSKTANSADLKKAYHKLAKQYHPDNAASGDTNAEKKFKEINAAYEVLKDEQKRAAYDRFGHDAFQNQQARGGAGSQGGHPFGADINDIFGDFFSDFMGGGGRRKPTSSKVRGSDLKYNLTINLEEAFHGVEKNISFSSEVKCDTCHGSGSEKGETTTTCDACGGVGATRVQQGFFMIEQTCHKCQGNGQIIKNPCKKCHGLGRYHKQRNLSVNIPAGVENGTRIRHPGEGEAGIRGGNNGDLYVDIAIKPHDIYKVDGANLHCKLPISFVNAALGGEVAVPVIEGGKVNLTIPAGTQNGDQLRLCGKGMSKIRSTIRGDMLAHVHVEVPKNLSKRQRELLEELRGESANEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.791 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDNKDAEEHFKEVKEAYEMLSDSQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGRGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRATFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTEHQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia mallei (strain NCTC 10247)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.549 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLHSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia mallei (strain NCTC 10229)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.549 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLHSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia mallei (strain ATCC 23344)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.549 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLHSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia mallei (strain SAVP1)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.549 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLHSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia pseudomallei (strain 1106a)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.568 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia pseudomallei (strain 1710b)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.597 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia pseudomallei (strain 668)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.568 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia pseudomallei (strain K96243)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.597 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNVGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRARGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWAACGVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.675 kDa
Sequence
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDSKDAEEHFKEAKEAYEMLSDSQKRAAYDQYGHAGVDPNMGAAGAQGFGGFADAFGDIFGDIFGQAAGGGRGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWASCGICHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPSGDLYVEIHIKPHPVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFTVAEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGPRHSPQSKSWFDRVKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.666 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKYHPDRNPGDKEAEASFKEVKEAYEILTDTDKKAAYDQFGHAGVDPNRGGGGFGGGGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVRGLTKELKVPTLVGCDSCDGSGAKKGSSATTCGTCHGMGQVQMRQGFFAVQQTCPTCHGRGKIIKDPCSKCHGNGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVTVREHPIFVRDGNNLYCEVPISFAKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLSERQKELLREFEASLTGESKKHSPKAEGFFDGVKKFFQDLNN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella frigidimarina (strain NCIMB 400)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.727 kDa
Sequence
MSKRDYYEVLGVGRDTSEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEIKEAYEILTDSDKKAAYDQFGHAGVDPNRGGHGGGQGDFGDIFGDVFGDIFGGGRRGGGQRQAARGSDLRYNLELSLEEAVRGLTKELRIPTLAACDLCDGSGAKKGTSATTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCGKCHGEGRVEKSKTLSVKIPAGVDTGDRIRLTGEGEAGEFGAPPGDLYVQVSVREHAIFTRDANNLYCEVPISFSKAALGGEIEVPTLDGKVSLKIPTETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNEKQKELLREFEATLTGESKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella halifaxensis (strain HAW-EB4)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.761 kDa
Sequence
MSKRDFYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGNKEAEASFKEVKEAYEILTDGDKKAAYDQFGHAGVDPNRGGGGFGGGADFGDVFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVRGLTKELRIPTLAACDACDGSGAKKGSSPTTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCNKCHGEGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEYGAPPGDLYVQVSVREHAIFQRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVNLKIPAETQTGRMFRMRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEDTLTGQSKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.607 kDa
Sequence
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKFHPDRNPGDKAAEASFKEVKEAYEILTDSDKKAAYDQFGHAGVDPNRGGGGFGGGADFGDVFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVRGLTKELRIPTLATCDLCDGSGAKKGSSPTTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCGKCHGEGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEFGAPPGDLYVQVTVREHAIFVRDGNNLYCEVPISFSTAALGGEIEVPTLDGKVNLKIPSETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLNDKQKELLREFDNTLTGSSKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.927 kDa
Sequence
MSKRDYYEVLGVGRDTSEREIKKAYKRLAMKFHPDRNPGDKEAEANFKEVKEAYEILTDSDKKAAYDQFGHAGVDPNRGGGGYGGSADFGDVFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVRGLTKELRIPTLAACDSCDGSGAKKGSSPTTCGTCHGQGQVQMRQGFFAVQQACPTCHGRGKIIKDPCNKCHGEGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEYGAPPGDLYVQVSVREHAIFQRDGNNLYCEVPISFSKAALGGEIEVPTLDGKVNLKIPAETQTGRMFRMRGKGVKSVRSHAVGDLLCKVVMETPVNLNERQKELLREFEDTLTGQSKKHSPKAEGFFDGVKKFFQDLNS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.584 kDa
Sequence
MAKRDYYEILGVDRGADKKEIKKAYRRLARKYHPDVSDDPDAAEKFKEISEAYAVLSDDEKRARYDRFGHAGMDGFSQEDIFNNINFEDIFSGLGFDIGNIFDMFGFGGGRRHGPQRGADISYTLDISLEDAYNGLETDIRVPHTKKCPVCHGSRAEPGTGTRTCQTCGGSGQVRQVRNTILGQMMNITTCPDCQGEGTVVEKPCSNCNGKGVVRKTSTIHVKVPAGVETGSRLRVPGEGEMGLRGGEPGDLYVVIKVKPHSIFRREGANLYTEKPISFVQAALGDTVEVPTLDRPVKLRIPAGTQSGTTFRVKGHGMPHLKWNGYGNLYVKVKVVTPRKLSPRQKELLREFASISGDEIHEDKGFFDKVKDAIIH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Stenotrophomonas maltophilia (strain R551-3)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.774 kDa
Sequence
MSKRDYYEVLGVARTANDEELKKAYRRCAMKFHPDRNPGDAAAEASFKECKEAYEVLSDGNKRRMYDSHGHAAFEHGMGGGGGPGGPDMNDIFGDIFGNIFGGAGGGGPRQARRGADIGYVMELDLEEAVRGVERRIEIPTLAECGDCDGSGSEDGKVETCNVCHGRGQVRIQRGIFAMQQACHNCGGRGQIIAKPCKTCHGNGRVEEDKVLSVKVPAGVDTGDRIRLSGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTNDQRKLLEQFEATFNGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.02 kDa
Sequence
MAKRDYYEVLGISKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGAGGGFGGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria monocytogenes serotype 4b (strain CLIP80459)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.036 kDa
Sequence
MAKRDYYEVLGVSKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGAGGGFSGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria monocytogenes serotype 4b (strain F2365)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.036 kDa
Sequence
MAKRDYYEVLGVSKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGAGGGFSGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria monocytogenes serotype 4a (strain HCC23)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.02 kDa
Sequence
MAKRDYYEVLGISKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEALSDPQKRAQYDQYGHVDPNQGFGGGAGGGFGGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAIFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCPTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDKVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.072 kDa
Sequence
MAKRDYYEVLGISKSASADEIKKAYRKLSKQYHPDINKEAGADEKFKEISEAYEVLSDSQKRAQYDQYGHVDPNQGFGGGAGGGFSGGGFSGFEDIFDTFFGGGGRQQDPNAPRQGSDLQYTMRLKFKEAVFGKDAEIEIPREENCDTCHGSGAKPGTTPEKCSHCGGKGSINVEQNTPFGRVVNKRTCQYCNGTGKEIKEKCSTCHGKGRVTKTKKIKVKVPAGVNDGQQMRVSGEGEAGINGGPNGDLYVVFVVIPDEFFEREADDIYVEVPITFVQATLGDEIDVPTVHGKVRLKIPSGTQTGTTFRLRGKGVPHLRGNGTGDQHVIVKVIVPKKLDDKQKEILREFASTTGDRVDEQTSGFFDKMKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
376 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.12 kDa
Sequence
MAKQDYYETLGVQKGADEKEIKRAYKRLAMKYHPDRTNGDKAAEEKFKEVNEAYEILMDKEKRAAYDQYGHAAFEQGGFGGGAGGFGGGFGGFGGFEDIFSEMFGGGASRQRVVRGEDLRYDIEITLEEAVRGTTKDIKINTLAACDHCDGSGAEKGSKVETCPTCHGHGRVRRQQGFFMTETTCPTCQGSGKKIEKPCKHCHGDGRVHKKKNLSVKIPAGVDTGNQLRLSGEGAAGENGAPAGDLYVVIHVKDHHIFERDGSNLYCEVPISFTMAALGGEIEVPTLDGRVKLKIPAETQTGKLFRMRGKGVTSTRAGYAGDLICKIIVETPVKLNEEQKELLRKFEESLEGQSKQRPKSSSFLDGVKKFFDNLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Azoarcus sp. (strain BH72)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.84 kDa
Sequence
MSKRDYYEVLGVNRDAGDDEIKKAYRKLAMKYHPDRNPDSKEAEEKFKEAKEAYEVLSDAQKKGAYDRYGHAGVDPSMGGGGGGQGFEGFADAFGDIFGDLFGGRGGGGGRSNVYRGADLRYNLEISLEEAARGAEKTIRIPTVEECGTCHGSGAKPGTQPKTCPTCGGAGQVRIQQGFFSIQQTCPKCHGTGRIIPDPCGDCGGAGRVKKQKTLEVKIPAGIDEGMRLRHSGHGEPGVNGGPPGDLYVEIHIRQHPVFERDHDDLHCEMPISFATAALGGEIEIPTLEGMARIKIPAETQSGKVFRLRGKGIKNVRSHTHGDLMCHVVVETPVNLTERQKELLREFEEVSKGDAERHNPKAKSWMDKVRDFFAT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.296 kDa
Sequence
MAKRDYYEVLGVERGAGEAELKKAYRRLAMKYHPDRNPDDKSAEEKFKEVNEAYEVLSDAGKRMAYDQYGHAGVDQSMGGGAGFGAGGANFSDIFGDVFSDFFGAGRAGARGGPQRGSDLRYTLELNLEEAVRGTTVTIRVPTLVHCKTCDGSGAKKGTTPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGSGKMIADPCPDCHGQGRVEEHKTLSVKVPAGVDSGDRIRLAGEGEAGTLGGPPGDLYVVVSVREHPIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPEGTQTGKLFRLRGKGVAPVRGGAAGDLMCRVVVETPVNLSKRQRELLEEFRGSLQGNSSHSPKASGWFEGMKRFFDDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.164 kDa
Sequence
MSDRGYYEVLGVSKGASDDEIKSAYRKLAIKYHPDKNKGDKEAEEKFKEATEAYEVLRDPQKRQAYDQFGKAGVNAGAGGGYGAGAYTDFSDIFGDFGDIFSEFFGGGGGGGSRGGGRRSGPQRGSDLRYNLEVSLEDAALGKEYKIEIPRLETCVDCTGSGASKGSSPTVCPDCSGTGQVRRTQGFFSVTTTCPRCKGKGKVISNPCKTCKGEGLTEKRRTIHIKIPAGVESGSRLKVSGEGESGPNGGPSGDLYVVTHIKKHPVFERQGNDLIVQKSISLSMACLGGEIEVPSIDGKTIQLKIPEGTESGQIFRLKGHGIPYLGSYGKGDQHVIIKVEIPKKLSKKQKELMEEFARESGEKVGSGGKSKLFFR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.164 kDa
Sequence
MSDRGYYEVLGVSKGASDDEIKSAYRKLAIKYHPDKNKGDKEAEEKFKEATEAYEVLRDPQKRQAYDQFGKAGVNAGAGGGYGAGAYTDFSDIFGDFGDIFSEFFGGGGGGGSRGGGRRSGPQRGSDLRYNLEVSLEDAALGKEYKIEIPRLETCVDCTGSGASKGSSPTVCPDCSGTGQVRRTQGFFSVTTTCPRCKGKGKVISNPCKTCKGEGLTEKRRTIHIKIPAGVESGSRLKVSGEGESGPNGGPSGDLYVVTHIKKHPVFERQGNDLIVQKSISLSMACLGGEIEVPSIDGKTIQLKIPEGTESGQIFRLKGHGIPYLGSYGKGDQHVIIKVEIPKKLSKKQKELMEEFARESGEKVGSGGKSKLFFR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain CbuK_Q154)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.085 kDa
Sequence
MAKRDYYEVLGVNRNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFDDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain Dugway 5J108-111)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.085 kDa
Sequence
MAKRDYYEVLGVNRNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFDDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain PCC 7424)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.744 kDa
Sequence
MPGDYYEILGVSRDANKDEIKRAYRRLARKYHPDVNKEIGAEERFKEINRAYEILSEPETRARYDRFGEAGVSSGAGSGFEYGDMGGIADIFETIFSGFGGMGTGTSSRRRTGPVRGDDLRLDFKLNFREAVFGGEKEIRIRHLETCQVCEGSGAKPGTGSRTCSTCSGSGQVRRATRTPFGTFAQVSVCPTCNGSGEVIEEKCEACGGSGRKQETKKLKITIPAGVDNGTRLRVSREGDAGQRGGPPGDLYVYLSVETDEEFQREGIDIKSEISISYLQAILGCRLSVNTVDGPEEITIEPGTQPNTVLTLPNRGVPKLGNPVARGDHLITINVSIPTRVNPEERELLEKLAKIRGESHGKGGIEGFLGGLFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain PCC 8801)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.52 kDa
Sequence
MSGDYYETLGVDRNASKEDIKRAYRRLARKYHPDINKEAGAEDRFKEINRAYEVLSEPETRARYDQFGEAGVSGAGAAGFDYGDMGGFADIFETIFSGFGGGVGTGSTRRRTGPTRGDDLRLDLKLDFREAIFGGEKEIRIPHLETCQVCNGSGAKPGTGSRTCSTCNGAGQVRRATRTPFGSFAQVSTCPDCNGAGQVIEQKCDACGGAGRKQETKKLKITIPAGVDNGTRLRVGKEGDAGTRGGTPGDLYVYLFVEPDKEFTREGMNIHSEITISYLQAILGCKLQINTVDGPQELVIPAGTQPNTELMLEDHGVPKLGNSAIRGDHLINVKIAIPTRINNEERELLEKLAHIKGQSHGKGGLEGFLGSLFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio alaskensis (strain G20)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.904 kDa
Sequence
MSQRDYYEVLGVSRDAADDEIKRAYRKKAMEFHPDRNPDNPEAEAKFKEAAEAYDVLRDAEKRARYDRFGHAGVNGNGYGGGGGFSSTEDIFAHFGDIFGDLFGFAGMGGARGPRPQAGSDLRYNLNISFRQAARGDEVTLRIPKNVTCPDCSGSGAAPGTQPETCPQCGGSGQVVRQQGFFQMAMPCSACRGEGRIVRNPCPRCRGAGQVQDIRELSVRIPAGVDTGNRLRLRGEGEPGVHGGPPGDLYVVIRVDDDKTFRRQGQDLVVRKEISFVQAILGDKVEVPTLDDPVTVDIPRGTQSGEVFRIAGKGLPHLGSSQTGALLVEVTVRIPSSVNDEQEKLLREFERLEENRPLRKVKNMFKKAGKAMGMD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas entomophila (strain L48)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.265 kDa
Sequence
MAKRDFYEVLGVERGASEGDLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDTSKRAAYDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGSRSGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCKPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFAVQQTCPRCHGQGKIITDPCNSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVINVREHDIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGAAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFEGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas mendocina (strain ymp)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.051 kDa
Sequence
MAKRDYYEVLGVERGASEAELKKAYRRLAMKYHPDRNPDDKGAEEKFKEANEAYEVLSDAGKRSAYDQYGHAGVDPQMGGGGGAGFGGANFSDIFGDVFSDFFGGGRGGSRGGAQRGSDLRYTLELDLEEAVRGTTVTIRVPTLVGCKTCDGTGAKKGTSPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGSGKMITDPCGSCHGQGRVEESKTLSVKVPPGVDTGDRIRLSGEGEAGTHGGPAGDLYVVVNVREHAIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPEGTQTGKLFRLRGKGVAPVRGGAAGDLMCRVAVETPVNLNKRQRELLDEFRKSLQGDDSHSPKASGWFEGVKRFFGDV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Ureaplasma parvum serovar 3 (strain ATCC 700970)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.841 kDa
Sequence
MAKRDYYEILGVSKSATPEEIKAAFRKLAKEHHPDRNKSADDTLFKEINEAYEVLSDSKKRAQYDQFGHDGPQGFSSASGFSGFSGGFGGVDFDINDIFGSFFNNASSSHNSSNQYETYDIHLRLHLDFMEAVNGISKNINYDRKITCHKCQGTGAKDPKDVKICTKCHGRGTSIENVHSLFGTIQQEVECHECEGTGKVASSKCEQCYGKKVINERVNLTVEIPAGTREGEKLLVSKKGNIVNNQEFDLYLHISVKPSKYFALDGLDIYSETYIDPIKAIVGGIIEVVTINGIKTIEIPSNTPEGKKFRISGSGIVNKKSNIFGKKNGDFYTTIRYAKPVELSKDEIAYLKNISTRTNQNVEYYKNKVLKEISK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.317 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKHHPDRNPGDAAAEAAFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECAPCHGSGSEDGKVETCGTCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLQQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain CbuK_Q154)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.085 kDa
Sequence
MAKRDYYEVLGVNRNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFDDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain Dugway 5J108-111)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.085 kDa
Sequence
MAKRDYYEVLGVNRNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFDDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain PCC 7424)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.744 kDa
Sequence
MPGDYYEILGVSRDANKDEIKRAYRRLARKYHPDVNKEIGAEERFKEINRAYEILSEPETRARYDRFGEAGVSSGAGSGFEYGDMGGIADIFETIFSGFGGMGTGTSSRRRTGPVRGDDLRLDFKLNFREAVFGGEKEIRIRHLETCQVCEGSGAKPGTGSRTCSTCSGSGQVRRATRTPFGTFAQVSVCPTCNGSGEVIEEKCEACGGSGRKQETKKLKITIPAGVDNGTRLRVSREGDAGQRGGPPGDLYVYLSVETDEEFQREGIDIKSEISISYLQAILGCRLSVNTVDGPEEITIEPGTQPNTVLTLPNRGVPKLGNPVARGDHLITINVSIPTRVNPEERELLEKLAKIRGESHGKGGIEGFLGGLFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain PCC 8801)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.52 kDa
Sequence
MSGDYYETLGVDRNASKEDIKRAYRRLARKYHPDINKEAGAEDRFKEINRAYEVLSEPETRARYDQFGEAGVSGAGAAGFDYGDMGGFADIFETIFSGFGGGVGTGSTRRRTGPTRGDDLRLDLKLDFREAIFGGEKEIRIPHLETCQVCNGSGAKPGTGSRTCSTCNGAGQVRRATRTPFGSFAQVSTCPDCNGAGQVIEQKCDACGGAGRKQETKKLKITIPAGVDNGTRLRVGKEGDAGTRGGTPGDLYVYLFVEPDKEFTREGMNIHSEITISYLQAILGCKLQINTVDGPQELVIPAGTQPNTELMLEDHGVPKLGNSAIRGDHLINVKIAIPTRINNEERELLEKLAHIKGQSHGKGGLEGFLGSLFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio alaskensis (strain G20)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.904 kDa
Sequence
MSQRDYYEVLGVSRDAADDEIKRAYRKKAMEFHPDRNPDNPEAEAKFKEAAEAYDVLRDAEKRARYDRFGHAGVNGNGYGGGGGFSSTEDIFAHFGDIFGDLFGFAGMGGARGPRPQAGSDLRYNLNISFRQAARGDEVTLRIPKNVTCPDCSGSGAAPGTQPETCPQCGGSGQVVRQQGFFQMAMPCSACRGEGRIVRNPCPRCRGAGQVQDIRELSVRIPAGVDTGNRLRLRGEGEPGVHGGPPGDLYVVIRVDDDKTFRRQGQDLVVRKEISFVQAILGDKVEVPTLDDPVTVDIPRGTQSGEVFRIAGKGLPHLGSSQTGALLVEVTVRIPSSVNDEQEKLLREFERLEENRPLRKVKNMFKKAGKAMGMD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas entomophila (strain L48)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.265 kDa
Sequence
MAKRDFYEVLGVERGASEGDLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDTSKRAAYDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGSRSGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCKPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFAVQQTCPRCHGQGKIITDPCNSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVINVREHDIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGAAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFEGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas mendocina (strain ymp)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.051 kDa
Sequence
MAKRDYYEVLGVERGASEAELKKAYRRLAMKYHPDRNPDDKGAEEKFKEANEAYEVLSDAGKRSAYDQYGHAGVDPQMGGGGGAGFGGANFSDIFGDVFSDFFGGGRGGSRGGAQRGSDLRYTLELDLEEAVRGTTVTIRVPTLVGCKTCDGTGAKKGTSPVTCTTCGGIGQVRMQQGFFSVQQTCPRCHGSGKMITDPCGSCHGQGRVEESKTLSVKVPPGVDTGDRIRLSGEGEAGTHGGPAGDLYVVVNVREHAIFQRDGKHLYCEVPISFADAALGGELEVPTLDGRVKLKIPEGTQTGKLFRLRGKGVAPVRGGAAGDLMCRVAVETPVNLNKRQRELLDEFRKSLQGDDSHSPKASGWFEGVKRFFGDV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Ureaplasma parvum serovar 3 (strain ATCC 700970)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.841 kDa
Sequence
MAKRDYYEILGVSKSATPEEIKAAFRKLAKEHHPDRNKSADDTLFKEINEAYEVLSDSKKRAQYDQFGHDGPQGFSSASGFSGFSGGFGGVDFDINDIFGSFFNNASSSHNSSNQYETYDIHLRLHLDFMEAVNGISKNINYDRKITCHKCQGTGAKDPKDVKICTKCHGRGTSIENVHSLFGTIQQEVECHECEGTGKVASSKCEQCYGKKVINERVNLTVEIPAGTREGEKLLVSKKGNIVNNQEFDLYLHISVKPSKYFALDGLDIYSETYIDPIKAIVGGIIEVVTINGIKTIEIPSNTPEGKKFRISGSGIVNKKSNIFGKKNGDFYTTIRYAKPVELSKDEIAYLKNISTRTNQNVEYYKNKVLKEISK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.317 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKHHPDRNPGDAAAEAAFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECAPCHGSGSEDGKVETCGTCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLQQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.538 kDa
Sequence
MSKRDYYDVLGVNRDASDDDIKKAYRKLAMKYHPDRNPDSKEAEDKFKEVKEAYEILSDSQKRGAYDQFGHAGVDPQAGMGGGGQGFGGFGDFADIFSDIFGGGRGGSGGGRSNVYRGADLRYNMEITLEEAARGCEKQIRIPSHESCSTCNGTGAKPGTQPKTCATCGGHGQVRMSQGFFSIQQTCPTCHGTGKQITDPCGSCHGAGQKKTTKTLNVKIPAGVDEGDRIRLGGEGEPGQNGGPAGDLYVVTHIKQHAVFQRDGMDLHCEMPISFSTAALGGEVEIPTLDGMAKVKISPETQSGRVYRLRGKGVKAVRGAEYGDLHCHVVVETPVKLTERQKELLREFEAISQGDVATHNPRSKSFMDKLRDFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium tetani (strain Massachusetts / E88)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.631 kDa
Sequence
MPKKDFYEVLGVEKGANDAEIKKAFRKLALKYHPDKNAGNKEAEERFKEINEAYQVLSDPQKRAQYDQFGTADFNGGGAGFSGFEDFDLGDIFESFFGGGFGGFGGSSRRRNGPQKGPDVQYSINLTFNEAVFGVEKEVSITKSETCETCTGTGAKPGTNSKTCPKCNGSGQIKVQRNTALGSFVSVNTCDMCGGKGTIISDPCSDCKGKGTVRKQKKIKVNIPAGVDTGNVIPIRGQGEAGVNGGPPGDLYISVRVMPDPFFKRRGDDIYIDQHISFAKASLGTELKVKTIDGEVKYDIPSGTQPGTVFRLKGKGVPHVNGRGRGDQYVNIIVDIPKSLNQKQKEALFAYMEASGEIQSSEKEGFFDKIKKNFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xanthomonas campestris pv. vesicatoria (strain 85-10)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.303 kDa
Sequence
MSKRDYYEVLGVARGASDEELKKAYRRCAMKHHPDRNPGDAAAEAAFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLVECAPCHGSGSEDGKVETCGTCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLQQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.951 kDa
Sequence
MARDYYEILGVSRDTDKEELKQAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSEPETRARYDRFGPEGVSGAGAGFQDVGDMGGFADIFESIFSGFAGGMGSPTQQRRRSGPARGDDLRLDLKLDFREAVFGGEKEIRISHLENCEVCSGSGAKPGTRPRTCSTCSGSGQVRRVTRTPFGSFTQVSTCPTCNGTGMVIEDKCDACDGKGANQVTKKLKITIPAGVDNGTRLRISSEGDAGQRGGPSGDLYVYLFVNEDEEFQRDGINILSEIKISYLQAILGCRLEVDTVDGPVELIIPAGTQPNTVMKLENRGVPRLGNPVSRGDHMLNVLIDIPNKVTPEERELLEKLAKIKGDRTGKGGLEGFLGNLFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.158 kDa
Sequence
MGKRDYYEILGIDKSASQDEIKKNYRKLARKYHPDVNKEADAAEKFKEVKEAYEVLSDDQKRAQYDQFGHSGPQSQGFGGFGGGAQDFGGFGDIFDMFFGGGGRSRDPNAPQQGNDLQYTMILDFEEAVFGKETDIEIPKEESCDTCNGSGAKPGTKPETCSHCHGSGQLNQEQNTPFGRVVNRRVCNYCQGTGKIIPDKCNTCGGSGTVQKNKKIHISIPAGIDEGQQIRVAGKGESGKNGGPAGDLFVVIKVRPHDFFVREGDHIFCELPLTYAQAALGDELEVPTVHGKVKVKVPAGTQTGKTFRIKGKGAPNVRGRGHGDQHIKIKVMTPTNLSEKQKDLLREFNELGGNESTDEQDDNIFQRFRRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Sinorhizobium medicae (strain WSM419)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.008 kDa
Sequence
MKRDLYETLGVQKSADEKELKSAFRKLAMKYHPDRNPGDNEAEKSFKEINEAYETLKDPQKRAAYDRYGHAAFEQGGMGNGFAGGGAHGFSDIFEDIFGEMMGGRQRRSSGGRERGADLRYNMEISLEEAYSGKTAQIRVPTSITCDVCTGTGAKPGTSPKTCGTCQGTGRVRAAQGFFSIERTCPTCGGRGQTITDPCTKCHGQGRVVEERTLSVNIPAGIEDGTRIRLSGEGEAGLRGGPAGDLYIFLSVKPHEFYQRDGADLYCAVPISMTTATLGGKFDVTTLDGTKSRVTVPEGTQAGKQFRLKGKGMPVLRSSQMGDLYIQIQIETPQKLTKRQRELLQEFEQISSKENNPESAGFFSRMKGFFDTLSE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.516 kDa
Sequence
MATRDYYEVLEISRTADDGEIKKSYRRLAMRYHPDRNPDDASAEERFKEISAAYEVLSDPQKRQAYDRFGHAGVNGGGGGPGAGFGGGGGGFGDVFSDLFEQAFGGGFRGQDSGRGADLRYELELTLEEAALGKEVTIQIPSSATCEVCRGSGAKPGSAVEDCATCGGRGQVRMVQGFFSVTRPCPQCNGSGKVIKEPCTNCHGHGRVRRNRDLQVKVPAGVDTGDRIRLNGEGEAGERGGPAGDLYIQVRVLPHALFERDGDDLHCAVPVQFTTMAMGGELEVPTLTGRAKVQIAPGTQSGAVFRLRGKGIKGVRSKLNGDLHCQLQVEVPVHLSARQKELLEEFAREGGDNIQHPQQESWWNKAKDFFDRMGL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Aggregatibacter actinomycetemcomitans
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.375 kDa
Sequence
MAKQDYYELLGISRSADEKEIKRAYKKLAMQYHPDRTKGDKEKEEKFKEIQEAYEVLNDKEKRAAYDQYGHAAFEQGTGFGGGSFGGADFGDIFGDMFGDIFGGGGRGRQRVVRGDDLRYDIEITLEEAVKGTTKDIKIHTLAPCDTCHGTGAEAGSKVETCPHCHGAGRLRRQQGFFVTEQPCHFCHGTGKKIEKPCKTCHGDGRVNKAKNLSVKIPAGVDTGNQLRLSGEGAAGENGAPAGDLYVVIHVKEHHIFERDGSNLYCEVPISFTMAALGGEIEVPTLDGRVKLKIPEETQTGKLFRMRGKGVTSTRSGYAGDLTCRIIVETPVKLNEEQKELLRKLEESLEGQTKQRPKSSSFLDGVKRFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia canadensis (strain McKiel)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.495 kDa
Sequence
MSQDYYQILGVSKTASSAELKKAYHKLAKQYHPDNAAAGDTNAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQSRRGAGGGTSSFHPDINDIFGDFFSDFMGGSRRSRPTSSKVRGSDLKYDLTINLEEAFHGIEKNISFSSEVQCDTCHGNGSEKGETITTCDACSGVGVTRIQQGFFTIEQTCHKCQGNGQMIKNPCKKCHGMGRYHKQRNLLVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDISIKPHDIYKVDGANLHCKLPISFVNAALGGEVEVPIIEGGKVNLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESMSEKENDSSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.994 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.994 kDa
Sequence
MAKRDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVMLKVPSETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Serratia proteamaculans (strain 568)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.825 kDa
Sequence
MAKKDYYEILGVSKTAEEREIKKAYKRLAMKFHPDRNQEQDAEARFKEIKEAYEILTDAQKRAAYDQYGHAAFEQGGMGGGGGFGGGAEFSDIFGDVFGDIFGGGRRQRASRGSDLRYNMELSLEEAVRGVTKEIRIPTLEECGVCHGSGAKPGSSPVTCPTCHGQGQVQMRQGFFTVQQACPHCHGRGQIIKDPCNSCHGHGRVEKAKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPAETQTGKLFRMRGKGVKSVRGGSQGDLLCRVVVETPVNLNDKQKQLLKELEESLGGPSGDKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.894 kDa
Sequence
MSKRDYYEVLGVGKSASKDEIKKAYRKLSKKYHPDINKEAGAAEKFKEVKEAYETLSDDQKRAHYDQFGHTDPNQGFGGGGFGGGDFGGFGFDDIFSSIFGGGARRRDPNAPRQGADLQYTMTLSFEEAAFGKETTIEIPREETCETCSGSGAKPGTKPETCSHCGGSGQLNMEQSTPFGKVVNRRVCHYCNGTGKQIKHKCSTCGGTGKVKKRKKINVTIPAGVDDGQQLRVAGQGEPGINGGPSGDLFVVFRVQEHEFFERDGDDIYCEMPLTFAQAALGDEIEVPTLHGKVKLKVPAGTQTGTKFRLKGKGVANVRGYGQGDQHIVVRVVTPTNLTENQKNILREFAEVSGNMPDEQEMSFFDKVKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus subtilis (strain 168)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.045 kDa
Sequence
MSKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEAGSDEKFKEVKEAYETLSDDQKRAHYDQFGHTDPNQGFGGGGFGGGDFGGFGFDDIFSSIFGGGTRRRDPNAPRQGADLQYTMTLSFEDAAFGKETTIEIPREETCETCKGSGAKPGTNPETCSHCGGSGQLNVEQNTPFGKVVNRRVCHHCEGTGKIIKNKCADCGGKGKIKKRKKINVTIPAGVDDGQQLRLSGQGEPGINGGPAGDLFVVFHVRAHEFFERDGDDIYCEMPLTFAQAALGDEVEVPTLHGKVKLKIPAGTQTGTKFRLRGKGVQNVRGYGQGDQHIVVRVVTPTNLTDKQKDIIREFAEVSGNLPDEQEMSFFDKVKRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.002 kDa
Sequence
MSKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKESGADEKFKEVKEAYEALSDDQKRAQYDQFGHTDPNQGFGGGFGGGGDFGGFGFDDIFSSIFGGGTRRRDPNAPRQGADLQYTMTLSFEDAAFGKETIIEIPREENCETCKGSGAKPGTKPDTCSHCGGSGQLNVEQNTPFGKVVNRRVCHHCEGTGKIIKNKCSDCGGTGKVKKRKKINVTIPAGVDDGQQLRVPGQGEPGVNGGPAGDLFVVFHVRAHEFFERDGDDIYCEMPLTFAQAALGDEVEVPTLHGKVKLKIPAGTQTGTKFRLRGKGVQNVRGYGQGDQHIVVRVVTPTNLTDKQKDIIREFAEVSGNLPDEQEMSFFDKVKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Blochmannia pennsylvanicus (strain BPEN)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.233 kDa
Sequence
MAKSDYYEILGISKNADEREIKKSYKRLAMKFHPDRNPGNTTAETKFKEIKEAYEVLSNSEKRAAYDQYGHAAFESGSMGATSNSGGADFSDIFGDVFGDIFGGNRRSRAGRGSDLRYNIELSLEDAVRGIIKEICIPTLSTCEKCRGTGARSNAAIITCMTCHGQGQVQIRQGFFSVQQSCPTCHGHGKIIKEACNKCHGNGRVERSKTLSVKIPSGVNTGDRIRLSGEGESGKNGAPSGDLYVQIQIRKHPIFDREEKNLYCEVPISFSMAALGGEIEVPTLDGRVKLKIPPETQTGKLFRMRGKGVKSVRSGGNGDLLCRVVVETPVKLNDIQKRLLQDLSDSFEGPHGNRNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Hahella chejuensis (strain KCTC 2396)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.541 kDa
Sequence
MAKRDYYEVLGVSRDVDGKEVKKAYRRLAMKYHPDRNPGDASAEEMFKEATEAYDVLSDDQKRAAYDQFGHAGVDGNAGAGGFGGGASFSDIFGDVFGDIFGGGGGGRTRANRGSDLRYTLDLDLEEAVRGTTVKIRVPSQVECKSCSGSGAEKGTQPETCGTCNGAGQVRMQQGFFSIQQTCPRCRGAGKIVRNPCRSCHGSGYVEEQKTLSVKVPAGVDTGDRIRLSGEGEPGVNGGPPGDLYVQVAVREHKIFTRDGRNLYCEVPISFVDAALGGELEVPTLDGRVKLKIPEETQTGRLFRLRGKGVTPVRGGAPGDLLCRVVVETPVNLTKKQKDLLREFQTSMEESGGQQAPKKHSWFEGVKSFFDDMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.072 kDa
Sequence
MATSKDYYEILGVSRDADQKEIKKAYRRLARKYHPDINKDDPDAEEKFKEISEAYEILSDPDKRARYDQYGHAGINEEDFNFEDFAQRGFGGFDDIFDMFFGGGMGRRRRGPRPGADLQYRMKIPFEDAAFGTTKKITIPRTETCDTCNGTGAKPGTSPKTCPQCNGSGQVRYTQRTPFGQFAQTRTCDRCGGRGTIIDDPCPTCQGSGKVRKQRKITVKIPPGVDTGTRLRMPNEGEAGDKGAPNGDLYIIIEVEPHDIFERKDDDIYCEVPISFVQAALGDKIEVPTLEGKVKFTIPEGTQPDTVFRLKNKGIPHLNGRGRGDEFIKVRVVIPEKMNDEQKELLRKFAEISGDEINPEQKSFIKKVKDAFGVG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.935 kDa
Sequence
MAKRDYYEVLGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKAAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGFNGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMDLTLEEAVRGVTKEIRIPTLEECDVCHGSGAKAGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCHKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPSETQTGKLFRMRGKGVKSVRGGSQGDLLCRVVVETPVGLSEKQKQLLKDLQESFGGPTGEKNSPRSKSFFDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.933 kDa
Sequence
MKRDLYEVLGVAKDADADEIKKAYRKLARQYHPDVNKEADAEEKFKEVKDAYDILSEPQKRAQYDRFGHQDPNQGFGGGGFDGSGMGGFGDIFDMFFGGNGRRANPNAPRKGSDLQFGLSIDFIDAIFGKETDVEIPKEAECDTCLGSGAKPGSGVDTCKTCSGTGQQEVVANTPFGRIVNRRVCSTCEGKGKVVKEKCSTCRGSGRVKVRRKIHLNIPAGVDDGAQLRVTGEGEPGANGGPPGDLYVVLRVKSHEFFEREGNDIYCEVPLTYAQAALGDEIEVPTVDGRVKLKIPAGTQTETFFRLRGKGVPHLRGNGRGDQHVKVRVITPTKLSDKQKELLRELAELSGEKPGQHGGEDEGFFEKMKRAFRGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Brevibacillus choshinensis
Length
375 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.958 kDa
Sequence
MKRDYYEVLGVGKGADADEIKKAYRKLARQYHPDVNKAADAEEKFKEVKEAYDVLSEPQKRAQYDRFGHQDPNQGFGGGGFDASGMGGFGDIFDMFFGGGGRRANPNAPRKGSDLQFGLSIEFTETVFGKETDVEIPKEAECDTCHGSGAKPGTGVETCKTCSGTGQQEVAANTPFGRIVNRRVCTTCEGKGKVFKEKCSSCRGSGRVKVRRKIHLNIPAGVDDGAQLRVTGEGEPGVNGGPPGDLYVVLRVKSHEFFEREGNDIYCEVPLTYAQAALGDEIEVPTVDGRVKLKIPSGTQTETFFRLRGKGVPHLRGNGRGDQHVKVRVITPTKLSDKQKELLRELAELSGEKPGQHGGEDEGFFEKMKRAFRGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Trichodesmium erythraeum (strain IMS101)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.589 kDa
Sequence
MARDYYEILGVSRSADKEELKRAYRRLARKYHPDVNKEPGSEERFKEINRAYEILSDPEMKARFDRFGEAGVSGGAASGFSTDFSDSFADIFESFFSGFGGAGTQGRRRTGPVRGDDLRLDLNLEFIEAIFGGDKELTIKHLETCGTCNGSGAKPGTKPQTCSTCGGTGQVRRATRTPFSSFTQVSVCPSCNGSGQIIEEKCVDCGGRGQKEATKKIKITIPGGVDNGTRLRVSNEGDAGRMGGPPGDLYVFLSVKNHPEFQRDGINIISQIKISYLQAILGCCLEINTVDGKTELTIPSGTQPNAILTLEDKGVPRLGNSVSRGAHLITIEIDIPTKITPEEKELLEKLAKIKGERTGKGGIEGFLGSWFQQK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain CbuG_Q212)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.917 kDa
Sequence
MAKRDYYEVLGVNRNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFGDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPMDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain RSA 331 / Henzerling II)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.886 kDa
Sequence
MAKRDYYEVLGVNLNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFGDIFGDIFSGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.856 kDa
Sequence
MAKRDYYEVLGVNLNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFGDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.379 kDa
Sequence
MARDYYDILGVSRDAGQEDLKQAYRRLARKYHPDVNKEAGAEERFKEINRAYEVLSDPETRARYDRFGEAGVSGAAAGYGDMGDMGGFADIFESIFSGFGGVGAGTSRRRTGPSRGDDLRFDLKLEFREAIFGGEKQIRITHLETCTTCNGSGAKPGTKPRTCGTCGGAGQVRRATRTPFGSFTQVSVCPTCNGKGQVIEDKCETCGGNGQAQVTKKLKITIPAGVDTGTRLRVSNEGDAGQQGGPAGDLYVYLFVQEDPEFRREGINILSEVKISYLQAILGSRLMVNTVDGEVELTIPPGTQPNTVLTLENHGVPRLGNPVSRGDHLITVLLEIPTRISAEERELLEKLAKIRGDRIGKGGIEGFFGKVFGG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.201 kDa
Sequence
MADFYQILGVSRDADANTLKSAYRKLARQYHPDVNKDPGAEDKFKEIGKAYEALADPETRARYDQFGEAGIGGAAGMPDMGDMGGFGDLFETFFNGFGGQSSQGGRSQRRGPQQGDDLRYDLNIDFKDAIFGQQREINIPHLETCEVCRGTGAKKGTGPTTCTTCGGSGQVRRATRTPFGNFTQVAECPTCNGVGQIISDPCTSCGGNGVKQVRKKLRINIPAGVDSGTKLRVSGEGNVGLKGGPPGDLYVFIKVKNDSNLKREGINIYSEISVSYLQAILGDTVDIITVDGKVNLKIPSGTQPNSTLSLENKGVPRLGNPVARGNHQVLVKVKLPTRITEDERNLLEDLASKYTEQNSSSNSGLFSRLFGKDS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.188 kDa
Sequence
MAKRDYYEVLGVERGSSDAELKKAYRRLAMKHHPDRNPGDKASEDMFKEANEAYEVLSDSSKRAAYDQYGHAGVDPSMGGGGGGFGGQNFSDIFGDVFSDFFGGGRGGSRGGAQRGSDLRYTLELNLEEAVRGTTVNIRVPTLVNCKPCDGSGAKKGSSPVTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIISDPCDSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTQGGPTGDLYVVINVREHAIFQRDGKHLFCEVPISFVDAALGGELEIPTLDGRVKLKIPEGTQTGKQFRIRGKGVAPVRGGGAGDLMCRVAVETPVNLSRRQRELLEELRGSLDDDNSHSPKTTGWFEGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas fluorescens (strain SBW25)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.34 kDa
Sequence
MAKRDYYEVLGVERGSSEADLKKAYRRLAMKHHPDRNPDSKESEEMFKEANEAYECLSDPNKRAAYDQYGHAGVDPSMGGGGAGFGGQNFSDIFGDVFSDFFGGGRGGQRGGAQRGSDLRYTLELNLEEAVRGTSVNIRVPTLVNCKPCDGSGAKKGSSPITCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIISDPCDSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTQGGPTGDLYVVINVREHSIFQRDGKHLFCEVPISFVDAALGGELEIPTLDGRVKLKIPEGTQTGKQFRIRGKGVAPVRGGGAGDLMCRVAVETPVNLGRRQRELLEEFRSSLEGDDSHSPKTTGFFDGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.124 kDa
Sequence
MSKRDYYEVLGVERGATEADLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDASKRAAFDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGGRGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCQPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIITDPCTSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVISVREHEIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFDGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas putida (strain GB-1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.11 kDa
Sequence
MSKRDYYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDASKRAAFDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGGRGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCQPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIITDPCTSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVISVREHEIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFDGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wigglesworthia glossinidia brevipalpis
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.467 kDa
Sequence
MAKSDYYDILGISKNASDREIKTAYKRLAVKFHPDRNPGNLEAESKFKEIKEAYEVLLDPKKRAAYNQYGHTAFDQGSSNTEFTSNADFSDIFGDVFGDIFGNNRRKRSNRGSDLQYNINLSLEEAVKGISKEITIPKLERCNICSGKGMQPGTSAQNCSTCNGQGQIQMRQGFFSVQQTCPSCRGKCKIIRFPCRNCSGQGRVERSKNISIRIPAGVDNGDKIRLSGEGEAGKLGGSSGDLYVKISVKEHPIFKREEHNLYCEVPINFAMAALGGDIEVPALDGRVKLRIPAETQTGRLFRMRGKGVKSIRSGHQGDLLCRVVVETPVRLSEKQKSLLKELGISFVGRTGMYNSPRSKSFFDGVKKFFDGLTN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.249 kDa
Sequence
MEEFDYYEILEIERSASGEEIKKAYRKMAMKYHPDRNEGSSEAEEMFKRVNEAYQVLSDEGKRQLYDRYGKQGLESQGYSGFSGRGFEDVFDDLGSIFDSVFGGGFSSSSRKRSGPKYNLDLAMELDLSFKEAIFGCKKEIKIRYKDACPDCKGTGAKEGKIETCPDCGGRGQVFIRQGFMTFAQTCPKCGGSGERIKEKCPKCNGKGHENKEENLEVSIPEGVDTDNRIRVSRKGHVGKNGERGDLYLVVRVEEDEHFMRHGNDIYLHVPLFFSTVPLGTTLKIPSLRGELELKIPPNTKDKEQFVFKNEGVKDVHSAKKGNLIAQVKIVYPAKINDEQRELLEKLSRSFGVEGTPHEKGFEGVFEKIKGWFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia sp. subsp. Brugia malayi (strain TRS)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.265 kDa
Sequence
MSKKDYYKLLGVDRNASTDEIKKAYKKLALKYHPDRNPGNKEAEEKFKEITAAYEVLSDSEKRAGYDRYGHEGASGGFDFSQGFGSAGDFSDIFNDFFGGEFGSSSRSKAKRSTTGVPGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDMCQGRGSEGATKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCNGSGRRRDEVNISVSIPKGIEEGAKVRVSGKGEAGAKGGKSGDLYVYVKITPHKIFTRNKADLHCKVPIRMTLAVLGGEIDVQSIDGAKIKVKVPEGTQTSTKLRCKEKGMPYMNSYARGDLYVQIIVETLNPNNLTKKQIELLKALEEEENASIQQQSEGFFSKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain CbuG_Q212)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.917 kDa
Sequence
MAKRDYYEVLGVNRNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFGDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPMDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain RSA 331 / Henzerling II)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.886 kDa
Sequence
MAKRDYYEVLGVNLNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFGDIFGDIFSGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.856 kDa
Sequence
MAKRDYYEVLGVNLNATEAEVKKAFRRLAMKYHPDRNPGDKDAEVKFKEAREAYEVLCDSRKRASYDQFGHAGVEQTFGGAGAGGFGFGDLGDIFGDIFGDIFGGARGGQAREQRGADLAYELVLSLEEAVHGLSRTIKVPTWINCKTCNGSGAKGSSPATCPRCNGSGQMRMQHGFLQVQQTCSVCRGRGQVIKDPCTDCHGQGRQQQTKTLSVKIPPGIDTGDRIRLAGEGEAGLFGAPPGDLYVQVRVKPHPLFHREGNDLHSEVPIDFTTAALGGEMEIPTLDGSVRLTIPPETQGGKQFRLRGKGVKALRSGAVGDLICHIVVETPVKLSPEQKDYLKQFAELLKKDEKNHSPRTRNWFDSVKDFFTSK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.379 kDa
Sequence
MARDYYDILGVSRDAGQEDLKQAYRRLARKYHPDVNKEAGAEERFKEINRAYEVLSDPETRARYDRFGEAGVSGAAAGYGDMGDMGGFADIFESIFSGFGGVGAGTSRRRTGPSRGDDLRFDLKLEFREAIFGGEKQIRITHLETCTTCNGSGAKPGTKPRTCGTCGGAGQVRRATRTPFGSFTQVSVCPTCNGKGQVIEDKCETCGGNGQAQVTKKLKITIPAGVDTGTRLRVSNEGDAGQQGGPAGDLYVYLFVQEDPEFRREGINILSEVKISYLQAILGSRLMVNTVDGEVELTIPPGTQPNTVLTLENHGVPRLGNPVSRGDHLITVLLEIPTRISAEERELLEKLAKIRGDRIGKGGIEGFFGKVFGG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.201 kDa
Sequence
MADFYQILGVSRDADANTLKSAYRKLARQYHPDVNKDPGAEDKFKEIGKAYEALADPETRARYDQFGEAGIGGAAGMPDMGDMGGFGDLFETFFNGFGGQSSQGGRSQRRGPQQGDDLRYDLNIDFKDAIFGQQREINIPHLETCEVCRGTGAKKGTGPTTCTTCGGSGQVRRATRTPFGNFTQVAECPTCNGVGQIISDPCTSCGGNGVKQVRKKLRINIPAGVDSGTKLRVSGEGNVGLKGGPPGDLYVFIKVKNDSNLKREGINIYSEISVSYLQAILGDTVDIITVDGKVNLKIPSGTQPNSTLSLENKGVPRLGNPVARGNHQVLVKVKLPTRITEDERNLLEDLASKYTEQNSSSNSGLFSRLFGKDS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.188 kDa
Sequence
MAKRDYYEVLGVERGSSDAELKKAYRRLAMKHHPDRNPGDKASEDMFKEANEAYEVLSDSSKRAAYDQYGHAGVDPSMGGGGGGFGGQNFSDIFGDVFSDFFGGGRGGSRGGAQRGSDLRYTLELNLEEAVRGTTVNIRVPTLVNCKPCDGSGAKKGSSPVTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIISDPCDSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTQGGPTGDLYVVINVREHAIFQRDGKHLFCEVPISFVDAALGGELEIPTLDGRVKLKIPEGTQTGKQFRIRGKGVAPVRGGGAGDLMCRVAVETPVNLSRRQRELLEELRGSLDDDNSHSPKTTGWFEGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas fluorescens (strain SBW25)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.34 kDa
Sequence
MAKRDYYEVLGVERGSSEADLKKAYRRLAMKHHPDRNPDSKESEEMFKEANEAYECLSDPNKRAAYDQYGHAGVDPSMGGGGAGFGGQNFSDIFGDVFSDFFGGGRGGQRGGAQRGSDLRYTLELNLEEAVRGTSVNIRVPTLVNCKPCDGSGAKKGSSPITCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIISDPCDSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTQGGPTGDLYVVINVREHSIFQRDGKHLFCEVPISFVDAALGGELEIPTLDGRVKLKIPEGTQTGKQFRIRGKGVAPVRGGGAGDLMCRVAVETPVNLGRRQRELLEEFRSSLEGDDSHSPKTTGFFDGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.124 kDa
Sequence
MSKRDYYEVLGVERGATEADLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDASKRAAFDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGGRGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCQPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIITDPCTSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVISVREHEIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFDGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pseudomonas putida (strain GB-1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.11 kDa
Sequence
MSKRDYYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDASKRAAFDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGGRGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCQPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIITDPCTSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVISVREHEIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFDGVKRFFGDL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wigglesworthia glossinidia brevipalpis
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.467 kDa
Sequence
MAKSDYYDILGISKNASDREIKTAYKRLAVKFHPDRNPGNLEAESKFKEIKEAYEVLLDPKKRAAYNQYGHTAFDQGSSNTEFTSNADFSDIFGDVFGDIFGNNRRKRSNRGSDLQYNINLSLEEAVKGISKEITIPKLERCNICSGKGMQPGTSAQNCSTCNGQGQIQMRQGFFSVQQTCPSCRGKCKIIRFPCRNCSGQGRVERSKNISIRIPAGVDNGDKIRLSGEGEAGKLGGSSGDLYVKISVKEHPIFKREEHNLYCEVPINFAMAALGGDIEVPALDGRVKLRIPAETQTGRLFRMRGKGVKSIRSGHQGDLLCRVVVETPVRLSEKQKSLLKELGISFVGRTGMYNSPRSKSFFDGVKKFFDGLTN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.249 kDa
Sequence
MEEFDYYEILEIERSASGEEIKKAYRKMAMKYHPDRNEGSSEAEEMFKRVNEAYQVLSDEGKRQLYDRYGKQGLESQGYSGFSGRGFEDVFDDLGSIFDSVFGGGFSSSSRKRSGPKYNLDLAMELDLSFKEAIFGCKKEIKIRYKDACPDCKGTGAKEGKIETCPDCGGRGQVFIRQGFMTFAQTCPKCGGSGERIKEKCPKCNGKGHENKEENLEVSIPEGVDTDNRIRVSRKGHVGKNGERGDLYLVVRVEEDEHFMRHGNDIYLHVPLFFSTVPLGTTLKIPSLRGELELKIPPNTKDKEQFVFKNEGVKDVHSAKKGNLIAQVKIVYPAKINDEQRELLEKLSRSFGVEGTPHEKGFEGVFEKIKGWFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia sp. subsp. Brugia malayi (strain TRS)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.265 kDa
Sequence
MSKKDYYKLLGVDRNASTDEIKKAYKKLALKYHPDRNPGNKEAEEKFKEITAAYEVLSDSEKRAGYDRYGHEGASGGFDFSQGFGSAGDFSDIFNDFFGGEFGSSSRSKAKRSTTGVPGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDMCQGRGSEGATKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCNGSGRRRDEVNISVSIPKGIEEGAKVRVSGKGEAGAKGGKSGDLYVYVKITPHKIFTRNKADLHCKVPIRMTLAVLGGEIDVQSIDGAKIKVKVPEGTQTSTKLRCKEKGMPYMNSYARGDLYVQIIVETLNPNNLTKKQIELLKALEEEENASIQQQSEGFFSKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.401 kDa
Sequence
MANKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNRGNKEAEEKFKEINEAYQVLSDPDKKANYDRFGTADFNGGGGFGDFSGGFGDFGDLGDIFNSFFGGGFSGGSSRARKDAPQRGNDMEYSISLTFEEAVFGVEKSINITRSENCETCGGTGAKKGTSPKTCDKCGGTGTIRVQRNTPLGSFVTQSSCDKCGGRGTIISDPCHECHGAGHVRKKRKISVKIPAGVDTGNVIPLRGQGEHGKNGGPAGDLYISIKVTPHKKFKREGFDIYIDTHISFPKAALGTDMTVPTIDGDVKYTIPAGTQSGTVFRLKGKGVQRVNGGGRGNQYVKVIVDTPKALNDKQREALKMFMEASGEAKSEKKSGFKRFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.344 kDa
Sequence
MAANKDYYDILGVSKDASDDEIKKAYRKLSKKYHPDINKAPDAEQKFKDVNEAYEVLGDSQKRAQYDQFGSADPNAGFGGGGFGGQGGFSDFGGGFEDIFGSFFGGGQRQSPNQPRQGEDLQYQMSLKFEEAIFGKKTTIKYSREALCKTCGGSGAKEGTSPVTCHKCNGTGTIQVTQNTPLGRMVRQQTCDVCNGTGKEIKEKCPTCGGTGHTSQQHEVKVSVPAGVEDGQQMRLQGQGEAGFNGGPYGDLYIIFQVQPSDMYERDGSEIYYNQTISFVQAALGDEIEVPTVHGKVKLKVPAGTQTGTNFRLKGKGAPRLRGNGTGDQHVKVKVTVPKKLNSGQKEALKQFAKASGEEPSGHGKSGFFDKFMN

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.044 kDa
Sequence
MSQRDYYEVLGVARDASEDEIKRQYRKLALQYHPDRNPDNPEAEQMFKEAAEAYDVLRDADKRARYDRFGHAGLNGNGGGHGFANADDVFAHFSDIFGDLFGFATGSSRMRGPRPQAGADLRYNLSISFRQAAKGDEVTLRLPKKVTCDECNGSGAAAGTKPETCRHCGGNGQIRQSQGFFQIAVPCPVCRGEGQVIPTPCPKCKGSGILQQVRELAVRIPAGVDTGNRLRLRGEGEPGLHGGPPGDLYVVVSVEQDKTFRRQGQDLVITHEVSFVQAALGDRIEVPTLDDPVTLDIPKGTQSGEVFRLTDQGLPYLGHHQKGDLLVEVRVLTPVSLTKKQEELLREFAKLEEGKPFEKVKKVARKIGKAMGME

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Dichelobacter nodosus (strain VCS1703A)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.046 kDa
Sequence
MADKDLYAILGVCRTANQDEIKKAYRKLSMKWHPDRNPNNKEEAEEKFKEINKAYEILSDSQKRASYDRFGFDAANQGAAGGGFSGGNFSDIFGDVFGDIFGNVRQTNGARQTRGHDLAYKIELSLEEAIHGVEKQIRIATQVRCGECHGSGMNAKSKKKTCPTCNGAGQVRMQQGFFSIAQPCPTCHGRGEIIENPCNKCQGTGRVKDTRVLTVNIPAGVDNGDRIRLSGEGEAGELGAPAGDLYIEIFVRAHPIFERQGNDLYCKMPISFTTACLGGDLEVPTLNGRVKLSIPEETQTGKTFRLKGKGVQSVRSNSVGDLYCTVTIETPINLSKAQKELLMNFEQALNEGGKTHTPQAKGFFDNIKQFFDNL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Sodalis glossinidius (strain morsitans)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.929 kDa
Sequence
MAKSDYYEILGVSRDAEEREIKKAYKRQAMKFHPDRNRGNAEAEAKFKEIKEAYEVLTDAQKRAAYDQYGHAAFEQGGMGGGGASGADFSDIFGDVFGDIFGGGRRQRVSRGADLRYNMELSLEEAVRGVTREIRIPTLEECDVCHGSGAKPGTSAVTCPTCHGQGQVQMRQGFFAIQQTCPTCQGQGKIIKDPCTKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEVGEHGAAAGDLYVQVQVCKHPIFEREENNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPAETQTGKLFRMRGKGVKSVRGGSQGDLLCRVVVETPVKLNERQKQLLRELEESFGGPSGDQNSPRSKSFLDGVKKFFDDLTR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Francisella philomiragia subsp. philomiragia (strain ATCC 25017)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.684 kDa
Sequence
MQQKCYYEILNVSKTASGVEIKRAYRKLAMKYHPDRNPDDKEAEIKFKEISEAYEILSDDGKRSRYDQFGHAGVNQQGGAGSAGGFGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTIEISLEEAFFGVEKEINIPRMESCDSCDGTGSKSKTKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGSSIADPCDDCYGSGKIKKQKTIKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYIQILVKEHKIFERRDMNLYCEMPISFTKACLGGEIKVPTLDGEVVLKVVPETQTGKVFRLRERGMKSLRGQRRGDLLCKVVVETPINLNSEQKELLEKFADSLGEDYQSKHSPKSKTWFDNVKDYAKKFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.729 kDa
Sequence
MQQKCYYEILNVSKTASGVEIKRAYRKLAMEYHPDRNPGDKEAEIKFKEISEAYEILSDDSKRSRYDQFGHAGVNQQSGFGGTGGFGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTLEITLEEAFFGVEKEITIPRMESCDSCDGTGSKSRSKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGYSITDPCDACYGNGKVKKQKTLKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYVQIIIKEHKIFERRDINLYCEMPISFTKACLGGDIKVPTLDGEVVLKVVPETQTGKVFRLREKGMKSLRGHRRGDLLCKVVVETPVNLSAEQKELLEKFADSLGEDYQSKHAPKSKTWFDNVKDYAKKFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.729 kDa
Sequence
MQQKCYYEILNVSKTASGVEIKRAYRKLAMEYHPDRNPGDKEAEIKFKEISEAYEILSDDSKRSRYDQFGHAGVNQQSGFGGTGGFGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTLEITLEEAFFGVEKEITIPRMESCDSCDGTGSKSRSKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGYSITDPCDACYGNGKVKKQKTLKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYVQIIIKEHKIFERRDINLYCEMPISFTKACLGGDIKVPTLDGEVVLKVVPETQTGKVFRLREKGMKSLRGHRRGDLLCKVVVETPVNLSAEQKELLEKFADSLGEDYQSKHAPKSKTWFDNVKDYAKKFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.458 kDa
Sequence
MATKLDYYAVLEVTRDANGDELKKAYRRLAMQYHPDRNPGDASAEARFKEINEAYDILKDEQKRAAYDRFGHAAFEGGGPGAGGFDFGGGLGDIFEQMFGDMMGGRRGGRRSGSDIQIQVSISFTEAFTGVKKPITVPTRVTCESCEGTGSADRDQGAETCPTCHGAGKVRAQQGFFLVERACPTCHGAGKVVRNPCAACHGAGTVERERTLEVAIPAGVEDGTRIRLSGEGEAGGKGAAPGDLYIHVAVEPHPIFQRDGANIYCRVPLRMSLAALGTEIEVPVVDGSRTKVKVPAGTQTGENFRLRGKGFSVLRSSARGDMYIQVSVETPRHLTKRQRELLEEFEAEAGDHERANPESTGFFSKVRDFFEGKL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia massiliae (strain Mtu5)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.357 kDa
Sequence
MMSQNYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRLGHDAFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSSRPTSAKVRGSDLKYNLTINLEEAFHGIEKNISFSSAVKCDTCHGSGSEKGETVTTCDACSGVGVTRMQQGFFTIEQACHKCQGNGHIIKKPCKKCHGMGRYHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDIAIKPHDIYKVDGAHLHCKLPISFVNAALGGEIEVPVIEGGKVKLTIPAGTQNGDQLRLRNKGMSKMRSTIRGDMLTHMHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Janthinobacterium sp. (strain Marseille)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.376 kDa
Sequence
MAKRDFYEILGVGKSASDEEIKKAYRKLAMKHHPDRNPDSKGAEDKFKEAKEAYEMLSDPQKRDAYDRYGHAGVDPNMGGGGGGGGFADAFGDIFGDIFGQAGGGRGGRGGPQVYRGADLRYNLEITLEQAAHGYDTTIRVPSWDNCETCDGSGAKPGTSPVNCTTCGGHGQVRMQQGFFSVLQTCPKCHGSGKINPSPCGTCSGAGKIKRNKTLEVKIPSGIDDGMRIRSSGNGEPGMNGGPPGDLYVEIRIKQHPMFQRDGDDLHCEIPISFAKAALGGEIEVPTLNGKASFTIPEGTQSGKTFRLRSKGIKGVRSGYAGDLFCHVIVETPVTLTERQKELMREFEQLTIEGGSKHSPQTKSWKDKVKEFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.508 kDa
Sequence
MEISYYEILEITQSADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGSGEKASEKCSDCKGLGYNESKDSVELNIPEGIDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFVRDDDDIYIEFPVFFTQAILGQSIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRIGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKIANWFKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.752 kDa
Sequence
MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSNSSGFGGFEDLGDIFSSFFGESFGSSSRRRKSSNDEKIPSDFIFNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGSGEKASEKCNDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNNTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGQSIKVPTIRGEVTLNLPKGAKDGQRFVLEKEGVKDVHSSRIGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKIANWFKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.659 kDa
Sequence
MEISYYELLEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSNSSGFGGFEDLGDIFSSFFGEGFGSSSRRRKSSNDEKIPSDFIFNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGSGEKASEKCSDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRMGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKITNWFKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Chelativorans sp. (strain BNC1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.197 kDa
Sequence
MKADFYETLCVSRNADEKELKSAFRKLAMQYHPDRNPGDMEAEKKFKEINEAYETLRDPQKRAAYDRFGHAAFEQGMGARGGFNGGGFADIFEDIFGDIMGGARQRRSGGRERGADLRYNMEITLEESFTGKTAQIRVPTAVTCDECAGSGARPGSSPVQCPMCHGAGRVRASTGGFFSIERTCPQCQGRGQIIDDPCRKCSGQGRLTEERSLSVNIPAGIEDGTRIRLAGEGEAGLRGGPPGDLYIFLSIKPHEFFQRDGADLYCKVPISMTTAALGGSFEVTTLDGTQTRVKVPEGTQSGRQFRLRGKGMPVLRQPQVGDLYIQVAVETPQNLTRRQRELLEEFEKISSGENSPQSTGFFARMKDFFETFGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Microcystis aeruginosa (strain NIES-843)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.698 kDa
Sequence
MPTDYYEILGVSRDAGKEDIKRAYRRLARKYHPDVNKEPGAEEHFKEINRAYEILSEPETRNRYDRFGEAGVSGGAAGFDPDNMGGFADIFETIFSGFGGMGGQATARRRTGPTRGEDLRLDFRLKFREAVFGGEKEIRIRHLETCQTCKGSGARPGTSSRTCTTCSGTGQVRRATRTPFGTFAQVSVCPTCDGAGEVIEEKCDVCGGSGRRQETKKLKITIPAGVDNGMKLRVAREGDAGLKGGPPGDLFVYLTVETDAEFQREGNDIKSDITISYIQAILGCTIKVNTVDGQEDLTIPAGTQPNTVLILENKGVPKLGNPVSRGDHRITVKISIPTRVTGEERELLEKLAKVRGETVGKGGIEGFLGNIFHK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Stenotrophomonas maltophilia (strain K279a)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.674 kDa
Sequence
MSKRDYYEVLGVARTATDDELKKAYRRCAMKFHPDRNPGDAAAEASFKECKEAYEVLSDGNKRRMYDSHGHAAFEHGMGGGGPGGPDMNDIFGDIFGNIFGGGGGGPRQARRGADIGYVMELDLEEAVRGVERRIEIPTLAECGDCDGSGSEDGKVETCNVCHGRGQVRIQRGIFAMQQACHNCGGRGQIIAKPCKTCHGNGRVEEDKVLSVKVPAGVDTGDRIRLQGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTPEQRKLLEQFEATFVGEEARKHSPKSATFMDGVKGFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.409 kDa
Sequence
MAKRDYYEVLGVAKNATDDELKKAYRKLAMKHHPDRNPDNKDAEEKFKEIKEAYEVLGDEQKRAAYDRYGHAGVDPNAAGMGGAGMGGGFADAFGDIFGEIFGGAGGRRGGAQVYRGADLKYALEITLEQAAHGFDTEIRVPSWEHCDTCHGSGAKPGTSPKTCRTCGGSGAVRMQQGFFSVQQTCPTCHGTGKEITDPCPSCDGVGRIRRNKTLQVKIPAGIDDGMRIRSSGNGEPGINGGPSGDLYVEIHIKPHKIFQRDGDDLHCELTIPFTTAALGGELQVPTLGGKAEISIPEGTQSGKTFRLRGKGIRGVRASYPGDLYCHVAVETPVRLSDEQKAILRQFETSLNDGGDRHSPQSKSWTDRVKEFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Herminiimonas arsenicoxydans
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.331 kDa
Sequence
MAKRDFYEILGLGKNASDEEIKKAYRKLAMKHHPDRNPDSKGAEDKFKEAKEAYEMLSDPQKRDAYDRYGHAGVDPNMGGGGGGGGFADAFGDIFGDIFGQAGGGRGGRGGPQVYRGADLRYNLEITLEQAAHGYDTTIRVPSWDSCETCDGSGAKPGTSPINCTTCGGHGQVRMQQGFFSVLQTCPKCHGSGKINPSPCTACSGAGKIKRNKTLEVKIPSGIDDGMRIRSSGNGEPGMNGGPPGDLYVEIRIKQHAMFQREGDDLHCEIPISFAKAALGGEIEVPTLNGKASFTIPEGTQSGKTFRLRSKGIKGVRSGYAGDLFCHVVVETPVTLTEKQKELLREFELLTIEGGSKHSPQTKSWKDKVKEFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.231 kDa
Sequence
MSKRDYYEVLGVSKDVSPQELKKAYRKVAMKYHPDRNSDDPNSEDKFKEASEAYEVLSDAQKRAAYDQYGHAGVDGNAGMGGGAGAGNFSDIFGDVFGDIFGGGGGRRRGGPSRGSDLRYTLDLSLEDAVKGTTVKIRVPTLVSCKPCGGSGAKPGTSPQTCTTCGGHGQVRMQQGFFSVQQTCPNCRGQGKMITDPCKECHGHGRVEETKTLSVKVPPGVDTGDRIRLAGEGEAGADGGPAGDLYVQVDVQDHAFFQREGRNLYCEVPISLFDACLGGELEVPTLDGRVKLKIPAETQTGKLFRLRGKGVTPVRGGAAGDLMCRVIIETPVNLTKKQKELLEELKASMKGEKNSPKQESWFEGMKNFFGDLKM

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.714 kDa
Sequence
MAKRDYYEVLGISRDADEKEIKRAYRKLAMKYHPDRNPDDKDAETKFKEASEAYEILADSSKRAAYDQFGHAGVDGQAGGGFGGGGASFSDIFGDVFGDIFGGGGRGRTTRGADLRYTLELDLEEAVKGKTVKINIPGHKECEACDGSGAEKGSRPETCGTCQGMGQVRMQQGFFTVQQACPTCRGSGQIIKNPCKSCHGQGRVRQEKTLSVKVPPGVDTGDRIRLSGEGEMGVDGGPPGDLYVQVAVREHSIFTRDGRNLYCEVPISIVDATLGGELEVPTLDGRVKLKIPPETQTGKLFRLRNKGVSPVRGGPAGDLLCRVIVETPVNLTKRQKELLEEFQQTLDGNNGTHHAPKKTSWFEGVKNFFDEMKF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Marinomonas sp. (strain MWYL1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.246 kDa
Sequence
MSKRDYYDVLGVAKDADKKDIKKAYRSLANKYHPDKNPDNPEALDKFKELAEAYEILSSDDKRAAYDRFGHDGVNGQAGGYGGAGAGGFSDIFGDVFGDIFGGGGGGQSRTRRGSDLRYTLELDLEQAVWGCEEKIRIPTLVNCKTCDGSGAKKGSTPKTCGTCGGAGQVRMSQGFFSVQQTCPECHGAGQVISDPCRDCHGQGRVQEYKTLNVKIPAGVDTGDRIRLSGEGEAGTHGGPAGDLFVQVSVKPHSIFERDGANLYCEVPISFTTAALGGEIDVPTLDGRVRLKVTAECQSGKLFRLRNKGVKPVRGGPVGDLICKVVVETPVNLTSRQKELFTELAESMGEGTDHSPKQKSWFDGVKRFFDDIKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
Length
374 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.873 kDa
Sequence
MAKRDYYEVLGVSKTSTEQEIKSAYRKLAKKYHPDMNKESGAEEKFKEVNEAASVLLDADKKAKYDQFGHAAFDGSSGFGGSGFGGFEDFFSNMGGGMDFGDIFSDLFGGGRSGRSSRRGPSKGQDIGLEATLTFKELVFGVNKKTILNLVKTCTKCDGVGAENPSDVHICTKCNGAGQIIVNKQMGPFQVQNQVTCDKCNGVGKEFKSKCKNCHGKGVESKREEVEIPLPKGLWPGQQFVMRGKGHASLEGGIPGDLYITIGIVKSDVFELIPNSNDLIMNYNISYLDAILGNEVIIKTLDGPVRLKIPKGVYSGQLIKVHDKGLYKNQTSDKRGDLLIKISISIPTSVSKEEKKILKELEQLSNFEPKNIID

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.261 kDa
Sequence
MARDFYEILGVSRSADAEELKRAYRRLARKYHPDVNKEPGAEEKFKEINRAYEVLSDPQARANYDRFGEAGVSGVGAAGFSDFGIGDMGGFADIFETFFGGFTTSSRRQQGPTRGEDLRYDLKLEFREAVFGGEKEIRINHLETCKTCQGTGAKPGTRPVTCSTCGGVGQVRRSARTPFGSFTQLTTCPTCGGSGVVIEDRCESCGGQGHIQVSKKLKITIPAGVDNGTRLRVSGEGDAGLRGGPPGDLYVYLFVQPDPEFQREGNNILSRIKISYLQAILGCRISVSTVDGEAELKIPAGTQPGTVLVLEGRGVPRVGNPVARGDHLITVDVEIPTHITHEERELLEKLAKIRGERLGKGGLEGFLGSLFGG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.05 kDa
Sequence
MAKKDYYEILGVSRNATQEEIRQAYKKLIKKWHPDRNYENKKLAEEKFKEIQEAYEVLSDPEKRAMYDKFGYVGDVPPNAGGGFRGFGGFEDIFKDFGDFINNDIFNIFFGDQRTSSRKRTKTPRKGEDINISVDVSFEELFTGVKIPLEYDRYEVCEHCHGEGVEPGSGWVTCPKCHGTGTVREERRTFLGVIVNQYTCNQCGGTGKIPGESCRVCGGTGRIRKRHRIEVNIPAGVENGTILRIQGGGHAGYYGGGYGDLYVHVRVVGYTSFERKGNNLIKDLKIDYVDAILGTKVKIKMPDGKIKEVKIPSGVQHGQEIYVYGEGIPDMRTGRRGDLILRINVGIPTKVSRTEKKLLKEIAKLRGKDVRED

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.83 kDa
Sequence
MSKRCYYEVLEVSREAQEGEIKRAYRKKAMEFHPDRNPGNAEAEEKFKEAAEAYDVLRDPEKRSRYDRFGHQGMNGMNGGFGGFQSSEDIFGAFGDIFGDIFGFGGGGRGANRMQAGSDLRYNLTVSFRDAAKGTEVELNIPVTDTCDTCEGSGSAPGTSPETCSHCGGRGAVEQNQGFFRISVPCPACNGRGKVITDPCSECRGAGYVRKQKDLNVRIPAGVDNGSRLRLRGEGEAGMNGGPHGDLYVVITVEPDKVFKRQGQDLVLSTEITFVQAALGYKLEVPTLDEPIEMDIPKGTQSGEVFQLRGLGLPYLGSSHKGDLLVEVKVKTPTGLNSRQEELLREFEALDEEKPMKKVKKLFKKAKDKVMGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.83 kDa
Sequence
MSKRCYYEVLEVSREAQEGEIKRAYRKKAMEFHPDRNPGNAEAEEKFKEAAEAYDVLRDPEKRSRYDRFGHQGMNGMNGGFGGFQSSEDIFGAFGDIFGDIFGFGGGGRGANRMQAGSDLRYNLTVSFRDAAKGTEVELNIPVTDTCDTCEGSGSAPGTSPETCSHCGGRGAVEQNQGFFRISVPCPACNGRGKVITDPCSECRGAGYVRKQKDLNVRIPAGVDNGSRLRLRGEGEAGMNGGPHGDLYVVITVEPDKVFKRQGQDLVLSTEITFVQAALGYKLEVPTLDEPIEMDIPKGTQSGEVFQLRGLGLPYLGSSHKGDLLVEVKVKTPTGLNSRQEELLREFEALDEEKPMKKVKKLFKKAKDKVMGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium botulinum (strain Alaska E43 / Type E3)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.521 kDa
Sequence
MANKDYYEVLGLQKGASDDEIKKAFRKLAIKYHPDKNKGNTEAEEKFKEINEAYQVLSDPEKKSNYDQFGSADFNGGGFGSGGFGGFDMGGFGDIFDMFTGGGSSTRRRNGPVNGNDIEYTLTLTFEEAVFGVEKEITVNRSESCEHCNGSGAEPGTSKKTCPTCSGTGQVRVQRQTPLGSFVSTSTCDRCSGTGNIIEKPCTHCRGNGNVRKTRKINVNIPAGVDTGNVMPLRGQGEHGLRGGSPGDLYIRINVSPSKEFTRKGNDIYIDTHISMAKAALGTEITVKTVEGNVKYTVPEGTQSGTLFRLKGKGVARVNSTGKGDQYVRVIVDIPKGLNQKQKEALYTFMEACGEEMDENTHSFKKNLFGRKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.507 kDa
Sequence
MANKDYYEVLGLQKGASDDEIKKAFRKLAIKYHPDKNKGNTEAEEKFKEINEAYQVLSDPEKKSNYDQFGSADFNGGGFGSGGFGGFDMGGFGDIFDMFTGGGSSTRRRNGPVNGNDIEYTVTLTFEEAVFGVEKEITVNRSESCEHCNGSGAEPGTSKKTCPTCSGTGQVRVQRQTPLGSFVSTSTCDRCSGTGNIIEKPCTHCRGNGNVRKTRKINVNIPAGVDTGNVMPLRGQGEHGLRGGSPGDLYIRINVSPSKEFTRKGNDIYIDTHISMAKAALGTEITVKTVEGNVKYTVPEGTQSGTLFRLKGKGVARVNSTGKGDQYVRVIVDIPKGLNQKQKEALYTFMEACGEEMDENTHSFKKNLFGRKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.433 kDa
Sequence
MSKRDYYEVLGVHRNASETEIKKAYRKLAIKYHPDKNAGDKAAEDKFKEISEAYSILSDTQQRVIYDQYGHAGLNGGGGGGGSYSSGGFGGTPFEDLFGDIFGDIFGGRGSQRSRGRRGDDLRYNLSINFEEAAFGLETKIQIPRHQTCGTCDGIGAKPGTTPRVCPTCQGAGQVRVQQGYFSLTRPCPECNGEGQIIDQPCEECHGSGRVRGKRTLSLKIPAGVETGSRLKLSSEGEPGLNGGPPGDLYVVISVQDHPLFQRDGQHVICEIPISFPQAALGCELEVPTLTEKVNVKVTPGTQSGKVIKLQGQGFPSLQGYARGDQLVVLRVEVPTSLTDRQKELLEEFAKEGGEEIHPMGKTFFDKVKELFG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.183 kDa
Sequence
MTIDYYETLSVERDADQGTIKKAYRKLAMKYHPDRNQGDKEAETLFKECTEAYEVLRDESKRRIYDTYGHEGLKNNGQRDTGGAGDIFSHFGDLFGFGGGGGRSQARRNGPIEGNDLRYDVSISFMESIQGVSKEVKLSRRETCWTCEGTGSRPGYQPQTCPTCNGRGQVLRSQGFFQVSTTCPECEGEGQVIKEPCNDCHGEGLVKKTKTVAIKIPAGVDTGARMRLRGEGEGGRRGGPSGDLFVIVHVSSHEFFERDGDTIYCRLPVSMTTAALGDTVDVPTVHGKKNLKIPAGSQSGERFTLRGEGVPSLRGRGNGDMVVELHVETPTGLCEEQKKMLRDFHSFCEEHGQHEKTKGFFAKLFDEVLGKNK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.602 kDa
Sequence
MSNQDFYATLGVARAATDDEIKKAYRKLAMKYHPDRNPDNKEAEEKFKEVQKAYETLSDKEKRAMYDQYGHAAFEGGGQGGFGGFGGFGGAQGFDFGDIFSQMFGGGSGRAQPDYQGEDVQVGIEITLEEAAKGVKKRINIPTYEACDVCNGSGAKPGASPETCPTCKGSGTVHIQQAIFRMQQTCPTCRGAGKHIKEPCVKCRGVGRNKAVKTVEVNIPAGIDDGQRIRLSGEGGPGMHGAPAGDLYVTVRIRAHKIFQRDGLDLHCELPISFAMAALGGELEVPTLDGKVKLTVPKETQTGRRMRVKGKGVKSLRSSATGDLYCHIVVETPVNLTDRQKELLEEFERISTGLENQTPRKKSFLDKLRDLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Neisseria meningitidis serogroup C (strain 053442)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.585 kDa
Sequence
MSNQDFYATLGVARTATDDEIKKAYRKLAMKYHPDRNPDNKEAEEKFKEVQKAYETLSDKEKRAMYDQYGHAAFEGGGQGGFGGFGGFGGAQGFDFGDIFSQMFGGGSGRAQPDYQGEDVQVGIEITLEEAAKGVKKRINIPTYEACDVCNGSGAKPGTSPETCPTCKGSGTVHIQQAIFRMQQTCPTCHGAGKHIKEPCVKCRGAGRNKAVKTVEVNIPAGIDDGQRIRLSGEGGPGMHGAPAGDLYVTVRIRAHKIFQRDGLDLHCELPISFATAALGGELEVPTLDGKVKLTVPKETQTGRRMRVKGKGVKSLRSSATGDLYCHIVVETPVNLTDRQKELLEEFERISTGLENQTPRKKSFLDKLRDLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.585 kDa
Sequence
MSNQDFYATLGVARTATDDEIKKAYRKLAMKYHPDRNPDNKEAEEKFKEVQKAYETLSDKEKRAMYDQYGHAAFEGGGQGGFGGFGGFGGAQGFDFGDIFSQMFGGGSGRAQPDYQGEDVQVGIEITLEEAAKGVKKRINIPTYEACDVCNGSGAKPGTSPETCPTCKGSGTVHIQQAIFRMQQTCPTCHGAGKHIKEPCVKCRGAGRNKAVKTVEVNIPAGIDDGQRIRLSGEGGPGMHGAPAGDLYVTVRIRAHKIFQRDGLDLHCELPISFATAALGGELEVPTLDGKVKLTVPKETQTGRRMRVKGKGVKSLRSSATGDLYCHIVVETPVNLTDRQKELLEEFERISTGLENQTPRKKSFLDKLRDLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.585 kDa
Sequence
MSNQDFYATLGVARTATDDEIKKAYRKLAMKYHPDRNPDNKEAEEKFKEVQKAYETLSDKEKRAMYDQYGHAAFEGGGQGGFGGFGGFGGAQGFDFGDIFSQMFGGGSGRAQPDYQGEDVQVGIEITLEEAAKGVKKRINIPTYEACDVCNGSGAKPGTSPETCPTCKGSGTVHIQQAIFRMQQTCPTCHGAGKHIKEPCVKCRGAGRNKAVKTVEVNIPAGIDDGQRIRLSGEGGPGMHGAPAGDLYVTVRIRAHKIFQRDGLDLHCELPISFATAALGGELEVPTLDGKVKLTVPKETQTGRRMRVKGKGVKSLRSSATGDLYCHIVVETPVNLTDRQKELLEEFERISTGLENQTPRKKSFLDKLRDLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.585 kDa
Sequence
MSNQDFYATLGVARTATDDEIKKAYRKLAMKYHPDRNPDNKEAEEKFKEVQKAYETLSDKEKRAMYDQYGHAAFEGGGQGGFGGFGGFGGAQGFDFGDIFSQMFGGGSGRAQPDYQGEDVQVGIEITLEEAAKGVKKRINIPTYEACDVCNGSGAKPGTSPETCPTCKGSGTVHIQQAIFRMQQTCPTCHGAGKHIKEPCVKCRGAGRNKAVKTVEVNIPAGIDDGQRIRLSGEGGPGMHGAPAGDLYVTVRIRAHKIFQRDGLDLHCELPISFATAALGGELEVPTLDGKVKLTVPKETQTGRRMRVKGKGVKSLRSSATGDLYCHIVVETPVNLTDRQKELLEEFERISTGLENQTPRKKSFLDKLRDLFD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Nitratiruptor sp. (strain SB155-2)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.667 kDa
Sequence
MVDIDYYELLEVDRNASFEEIKKAYRKLALKYHPDRNPDNPEAEEKFKLINEAYQVLSDEEKRALYDQYGKAGLENQGFSGFNQKSFDDIMDFFESVFGETFGGGFGSRRRSDEKYPLDLSIEMEISFQEALFGTQKEVHYSFKVPCSACKGTGAKDGKLTACPECHGRGQIYYRQGFMTFSQTCPRCHGQGEVAQEHCEECSGKGYRIEKEKITIDIPEGIDSGNRIRAQSRGNVSASGMRGDLYITVFVQEDDHFVRYNDDIYMEVPIFFTQAALGETITIPTPRGERELQLNVGTKDKEQFVFKGEGFKNVHTGKKGNLIAQVKIIYPTSLNDEQKELLHKLQESFGVESKPHEEKFSSIFEKVKNWFTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.444 kDa
Sequence
MAADKRDYYEVLGVHKNASDTEIKKAFRKLAIQYHPDKNPDDKEAEEKFKEITEAYEVLSDPQKRAQYDQFGHAGVGAGGFSGGGFGGFGAGTPFGDIFGDIFGDIFGGRPRGSRGRRGDDLQYNMELSFEEAAFGAEKEIQVPYGKRCGDCGGSGAKPGTEPKVCPTCRGAGQVRFQQGFFSVSKTCNHCNGEGRVVENPCTSCRGSGMIRDTKTLSVKVPAGVETGTRLKLSGEGGQGIKGGGNGDLYVAIAVREHPIFTREDNDVLCEIPVSFVQAALGCEIEVPTLDGKVSMKIPEGTQSGRIFRLRGKGVPQLQGYGRGDQLVIIKVETPSNLNKRQRELLEEFARISGEDVHPMKKSFFDKVMDFIS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia africae (strain ESF-5)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.131 kDa
Sequence
MSQNYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRLGHDAFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSSRPTSAKVRGSDLKYNLTINLEEAFHGIEKNISFSSAVKCDTCHGSGSEKGETVTTCDACSGVGATRMQQGFFTIEQACHKCQGNGHIIKNPCKKCHGMGRYHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDITIKPHDIYKVDGANLHCKLPISFVNAALGGEIEVPVIEGGKVNLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.131 kDa
Sequence
MSQNYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRLGHDAFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSSRPTSAKVRGSDLKYNLTINLEEAFHGIEKNISFSSAVKCDTCHGSGSEKGETVTTCDACSGVGATRMQQGFFTIEQACHKCQGNGHIIKNPCKKCHGMGRYHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDITIKPHDIYKVDGANLHCKLPISFVNAALGGEIEVPVIEGGKVNLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.523 kDa
Sequence
MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGIGEKASEKCSDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRMGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKITNWFKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter jejuni (strain RM1221)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.474 kDa
Sequence
MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGIGEKASEKCSDCKGLGYNESKNSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRIGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKIANWFKS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.954 kDa
Sequence
MELNYYEILEISQTSDKETIKKAYRKMALKYHPDRNQGDKEAEEKFKLVNEAYEVLSNDEKRSIYDRYGKEGLKGQAGGFGGFGDVDLGDIFSSFFGDGFGFGSSTRKKEKGNKYPQDLKITTKISFKEAVFGCKKKIDFSYKSFCKSCKGSGSENGKLDTCPHCGGKGQVGVRQGFMTFVQSCDHCKGSGQIIKDKCKTCHGNGYEEIKDHIELDIPEGIDSGMSLRVQNKANELPNSSQRGDLYIKIIVEDDDKFIRHDDDIYTIVPVFFTQAALGKTIKVSTIRGEADLKLPVGAKDKQKFELTNEGVKNIHNGKLGSHIVQIEIKFPKNLTDEQKNLLLQLEKSFGLADEEAFIEQESLFDKIKSWFSH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.709 kDa
Sequence
MAKRDYYEVLGVNRDATDEEIKKAYRKLAMKYHPDRNPDNPKAEEHFKEAKEAYEVLSDDQKRAAYDQYGHAGVDPSAAAGAGAGGFGNFADAFGDIFGDIFGGGGGGRRSNVYRGADLRYNMEISLEEAARGTETKIRIPVMAECETCHGSGARPGTQPVTCSTCGGHGQVRMQQGFFSVQQTCPKCHGSGKMVKDPCPTCHGGGRVKQHKTLSVKIPAGVDEGDRIRLSGEGEAGVNGGPPGDLYVVVHLKKHPIFERDGANLHCEMPISFTTAALGGEIEIPTLDGHAKMKVPPETQTGAVFRLRGKGIKPLRSNEHGDLFCHVIVETPVKLTERQKELLRELEDINQQDSGKHSPREKSWMTKVKDFFQ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.564 kDa
Sequence
MKKDYYEILGLTKSASKDEIKKAYRTLAKTYHPDVNKETNAEEKFKEITEAYEILNDDVKREQYNQFGHAAFDPNAGGFGGQNPFTNAEGFSGFSDFSGFGSIFTDFFGGFGNSQRANPNRAQRGEDRHAVIKISFIDSVLGKEIVEPLEKFETCNTCNGSGAKSQSDIITCTQCSGMGEQIKITKTFLGQMQQNVICSKCNGIGKEIVEKCLICKGKTHTKTTKNITIKIPAGIQNGQTLRVENYGNAGLNGGSNGNLILSIKVSPHKHFVRKNNDIILRLPVSIKSVIGSEKVEVPTPYGFEIIKIDPNIKTGDELIIKNKGIITKYESGKMIVIFEIFIPKLTSFEKKEISTILEKNADKFYEKWIKEFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bordetella avium (strain 197N)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.255 kDa
Sequence
MAKRDYYEVLGVAKDAADDELKKAYRKLAMKYHPDRNPGNKEAEEKFKEAKEAYEVLGDEQKRAAYDRYGHAGVDPNSAGGAGMGGGFADAFGDIFGEIFGAGRRGGGGGPQVYRGADLKYALEITLEQAANGFETEIRVPSWENCDTCHGSGAKPGTTPKTCRTCGGSGAVRMQQGFFSVQQTCPTCHGSGKEITDPCTSCDGVGRTRRNKTLQVKIPAGIDDGMRIRSAGNGEPGVNGGPPGDLYVEIHIKQHRIFQRDGDDLHCELTIPFTTAALGGELQVPTLGGKAEISIPEGTQSGKTFRLRGKGIRGVRAGYPGDLYCHIVVETPVRLSDEQKNILRQFEASLNDGGDRHSPQSKSWTDRVKEFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.249 kDa
Sequence
MAKRDYYEVLGVAKNASDEDLKKAYRKLAMKYHPDRNPDSKEAEEKFKEAKEAYEVLGDEQKRAAYDRYGHAGVDPNAAGMGGGMGGGFADAFGDIFGEIFGAGRRGGGGPQVYRGADLKYALEITLEQAASGFDTEIRVPSWENCDTCHGSGAKAGTSPKTCRTCGGSGAVRMQQGFFSVQQTCPTCHGTGKEITDPCPSCDGVGRTRRNKTLQVKIPAGIDDGMRIRSSGNGEPGINGGPPGDLYVEIHIKQHKIFQRDGDDLHCELTIPFTTAALGGELQVPTLGGKAEISIPEGTQSGKTFRLRAKGIRGVRGSYPGDLYCHVVVETPVRLSDEQKAILRQFEASLNDGGDRHSPQSKSWTDRVKEFFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Haemophilus somnus (strain 129Pt)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.013 kDa
Sequence
MAKRDYYEILGVQKGADDKEIKRAYKRLAMKYHPDRTKGDKESEEKFKEINEAYEVLADKEKRAMYDQYGHAAFEQGGGAGGFGGFSGADFGDIFGDMFGDIFGGGRSRQRVVRGEDLRYDIEISLEEAVKGCKKDIQINTLVHCGTCHGSGAEAGSKIESCPTCHGAGRVRRQQSFFVTEQTCPHCHGTGKKIEKPCHTCHGEGRVHKTQNLTVTIPMGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVKKHHIFERDGNNLYCEVPISFTMAALGGEVEIPTLDGRLKVKIPAETQTGKLLRLRGKGITSRGYAGDLICEIVIETPIKLNEEQKELLRKLEESLEGKTLQRPKSSGFLDGVKKFFDNLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Histophilus somni (strain 2336)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.043 kDa
Sequence
MAKRDYYEILGVQKGADDKEIKRAYKRLAMKYHPDRTKGDKESEEKFKEINEAYEVLADKEKRAMYDQYGHAAFEQGGGAGGFGGFSGADFGDIFGDMFGDIFGGGRSRQRVVRGEDLRYDIEISLEEAVKSCKKDIQINTLVHCGTCHGSGAEAGSKIESCPTCHGAGRVRRQQSFFVTEQTCPHCHGTGKKIEKPCHTCHGEGRVHKTQNLTVTIPMGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVKKHHIFERDGNNLYCEVPISFTMAALGGEVEIPTLDGRLKVKIPAETQTGKLLRLRGKGITSRGYAGDLICEIVIETPIKLNEEQKELLRKLEESLEGKTLQRPKSSGFLDGVKKFFDNLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia peacockii (strain Rustic)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.134 kDa
Sequence
MSQNYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQTRAAYDRLGHDAFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSSRPTSAKVRGSDLKYNLTINLEEAFHGIEKNISFSSTVKCDTCHGSGSEKGETVTTCDACSGVGATRMQQGFFTIEQACHKCQGNGHIIKNPCKKCHGMGRYHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDITIKPHDIYKVDGANLHCKLPISFVNAALGGEIEVPVIEGGKVNLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia rickettsii (strain Iowa)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.073 kDa
Sequence
MSQNYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKAINAAYDVLKDEQKRAAYDRLGHDAFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSSRPTSAKVRGSDLKYNLTINLEEAFHGIEKNINFSSAVKCDTCHGSGSEKGETVTTCDACSGVGATRMQQGFFTIEQACHKCQGNGHIIKNPCKKCHGMGRYHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDITIKPHDIYKVDGANLHCKLPISFVNAALGGEIEVPVIEGGKVSLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia rickettsii (strain Sheila Smith)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.072 kDa
Sequence
MSQNYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKAINAAYDVLKDEQKRAAYDRLGHDAFQNQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGSRRSSRPTSAKVRGSDLKYNLTINLEEAFHGIEKNINFSSAVKCNTCHGSGSEKGETVTTCDACSGVGATRMQQGFFTIEQACHKCQGNGHIIKNPCKKCHGMGRYHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDITIKPHDIYKVDGANLHCKLPISFVNAALGGEIEVPVIEGGKVSLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.212 kDa
Sequence
MAKRDYYEVLGVNKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDENKRVNYDQFGHDGPQGGFGSQGFGGSDFGGFEDIFSSFFGGGSRQRDPNAPRKGDDLQYTMTITFEEAVFGTKKEISIKKDVTCHTCNGDGAKPGTSKKTCSYCNGAGRVSVEQNTILGRVRTEQVCPKCEGSGQEFEEPCPTCKGKGTENKTVKLEVTVPEGVDNEQQVRLAGEGSPGVNGGPHGDLYVVFRVKPSNTFERDGDDIYYNLDISFSQAALGDEIKIPTLKSNVVLTIPAGTQTGKQFRLKDKGVKNVHGYGYGDLFVNIKVVTPTKLNDRQKELLKEFAEINGENINEQSSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
373 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.159 kDa
Sequence
MAKRDYYEVLGVNKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDENKRANYDQFGHDGPQGGFGSQGFGGSDFGGFEDIFSSFFGGGSRQRDPNAPRKGDDLQYTMTITFEEAVFGTKKEISIKKDVTCHTCNGDGAKPGTSKKTCSYCNGAGRVSVEQNTILGRVRTEQVCPKCEGSGQEFEEPCPTCKGKGTENKTVKLEVTVPEGVDNEQQVRLAGEGSPGVNGGPHGDLYVVFRVKPSNTFERDGDDIYYNLDISFSQAALGDEIKIPTLKSNVVLTIPAGTQTGKQFRLKDKGVKNVHGYGHGDLFVNIKVVTPTKLNDRQKELLKEFAEINGEDINEQSSNFKDRAKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.258 kDa
Sequence
MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVSGGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRSSGFGGGRRSGPQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCVDCNGSGASKGSSPATCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTIISNPCRSCGGQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGPHGDLYVVTHIKKHELFERQGNDLILVRKISLAQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGMPYLGAYGKGDQHVIVKIEIPKKITRRQRELIEEFARESGENIPGSKGKIFTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.258 kDa
Sequence
MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVSGGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRSSGFGGGRRSGPQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCVDCNGSGASKGSSPATCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTIISNPCRSCGGQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGPHGDLYVVTHIKKHELFERQGNDLILVRKISLAQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGMPYLGAYGKGDQHVIVKIEIPKKITRRQRELIEEFARESGENIPGSKGKIFTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.943 kDa
Sequence
MSKRDYYEVLGVAKNASDEEIKKAYRKLAMKHHPDRNPGDHAAEDKFKEAKQAYEILSDSDKRAAYDQFGHAGVDPQSGMGGGGFGGGGFSDAFSDIFGDIFGGGGGNRRDRVYRGADLRYNLEIGLEEAARGTETKIRIPTLEECGTCHGSGAKPGTQPTTCSACGGHGQVRVQQGFFSVQQTCPRCGGTGKMVSDPCPSCHGEGRVKKHKTLSVKIPAGVDSGDRIRLAGEGEAGVNGGPSGDLYVVIHLKDHPVFKRDGDDLHCEMPISFATAALGGEVEIPTLDGHAKIKIPAETQSGKVFRLRGKGIKGVRSHAPGDLLCHMLVETPVNLSERQRELLREFEALSPGRNNNPRAQSFMDKVKSFFGT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia pipientis wMel
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.817 kDa
Sequence
MSKKDYYDLLEVGRNASIDEIKKAYKKLALRYHPDRNPGNQEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHEGASGGFQGFSSAGDFSDIFNDFFGGGFGGGASRSRAKRSTTGVSGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDTCQGTGGEGAIKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRRRDEVNISVSIPKGIEEGAKVRISGKGEAGTKGGKSGDLYVYVKIIFHKIFARNKADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTKKQIELLKALEEEENASVQQQSEGFFSKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia pipientis subsp. Culex pipiens (strain wPip)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.875 kDa
Sequence
MNKKDYYDLLEVSRNASTDEIKKAYKKLALKYHPDRNPGNKEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHDGASGGFDFSQAGGDFSDIFNDFFGGGFGGSTSRSRTKRSTTGVSGADLRYDLKITLEDAFKGIQAPIHYVTNIKCNTCQGTGSEGAIKPVQCNTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRKRDEVNISVSIPKGIEEGAKVRVSGKGEAGARGGKSGDLYVCVKIATHQIFTRNRADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTQKQIELLKALEEEEHESVEQKSEGFFGKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia sp. subsp. Drosophila simulans (strain wRi)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.789 kDa
Sequence
MSKKDYYDLLEVGRNASIDEIKKAYKKLALKYHPDRNPGNQEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHEGASGGFQGFSSAGDFSDIFNDFFGGGFGGGASRSRAKRSTTGVSGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDTCQGTGGEGAIKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRRRDEVNISVSIPKGIEEGAKVRISGKGEAGTKGGKSGDLYVYVKIIFHKIFARNKADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTKKQIELLKALEEEENASVQQQSEGFFSKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia pipientis wMel
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.817 kDa
Sequence
MSKKDYYDLLEVGRNASIDEIKKAYKKLALRYHPDRNPGNQEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHEGASGGFQGFSSAGDFSDIFNDFFGGGFGGGASRSRAKRSTTGVSGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDTCQGTGGEGAIKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRRRDEVNISVSIPKGIEEGAKVRISGKGEAGTKGGKSGDLYVYVKIIFHKIFARNKADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTKKQIELLKALEEEENASVQQQSEGFFSKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia pipientis subsp. Culex pipiens (strain wPip)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.875 kDa
Sequence
MNKKDYYDLLEVSRNASTDEIKKAYKKLALKYHPDRNPGNKEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHDGASGGFDFSQAGGDFSDIFNDFFGGGFGGSTSRSRTKRSTTGVSGADLRYDLKITLEDAFKGIQAPIHYVTNIKCNTCQGTGSEGAIKPVQCNTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRKRDEVNISVSIPKGIEEGAKVRVSGKGEAGARGGKSGDLYVCVKIATHQIFTRNRADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTQKQIELLKALEEEEHESVEQKSEGFFGKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Wolbachia sp. subsp. Drosophila simulans (strain wRi)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.789 kDa
Sequence
MSKKDYYDLLEVGRNASIDEIKKAYKKLALKYHPDRNPGNQEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHEGASGGFQGFSSAGDFSDIFNDFFGGGFGGGASRSRAKRSTTGVSGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDTCQGTGGEGAIKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRRRDEVNISVSIPKGIEEGAKVRISGKGEAGTKGGKSGDLYVYVKIIFHKIFARNKADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTKKQIELLKALEEEENASVQQQSEGFFSKVKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Pasteurella multocida (strain Pm70)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.776 kDa
Sequence
MAKKDYYDVLGVERGADEKEIKRAYKKLAMKYHPDRTQGNKELEEKFKEIQEAYEVLSDKQKRANYDQYGHAAFEQGGFGGGGFSGADFGDIFGDMFGDIFGGGRARQRVVRGDDLRYDLEISLEEAVRGTTKDIQINTLAHCDSCDGSGAEKGSKVETCSTCHGAGRVRRQQGFFVTEQVCPSCHGSGKKIEKPCKSCHGDGRVHKKKNLSVKIPAGVDTGNQLRLSGEGAAGENGAPNGDLYVVIHVRDHHIFERDGSNLYCEVPISFTMAALGGEIEVPTLDGRVKLKIPAETQTGKLFRMRGKGVTSARSAYAGDLICKIIVETPVKLNEEQKALLRQLEESLEGSSNKPKSSSFFDGVKKFFDNLGK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.82 kDa
Sequence
MAKRDYYEVLGVSKTASEKEIKKAYKRLAMKYHPDRNQGDKEAESQFKEVKEAYEILTDDQKRAAYDQYGHAAFEQGGMGGGGADFSDIFGDVFGDIFGGGRRQQRPSRGADLRYSMELTLEEAVRGVTKEIRIPTLETCDICHGSGAKAGTSPVTCSTCQGAGQVHMRQGFFTVQQPCPHCHGRGQIIKDSCHKCHGHGRVERYKTLSVKIPAGVDTGDRVRLSGEGEAGAKGAPAGDLYVQVQVKSHHIFERQESNLYCEVPVNFAMAALGGEIEVPTLDGRVKLKIPAETQTGKMFRMKGKGVKSVRGGVQGDLLCRVVVETPVKLNERQKELLRELGESFGGAGEETNSPRSKSFFDGVKKFFDDLTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Arcobacter butzleri (strain RM4018)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.75 kDa
Sequence
MTEIDYYELLEISRNSDKSTIKKAYRQMAMKYHPDKNPGDNEAEEKFKAINEAYQVLSDDEKKSIYDRYGKAGLEGHGQRGGGFSGGFDDLGSIFEEMFGFGTSSRSRRERKTYNYNLDVTIEVKLEFNEAVFGCNKEINYKYKTACKPCEGTGAKDGKLSTCPTCKGQGQVHSRQGFMTFAQTCPRCGGTGQATTDSCKSCKGTGYEEVKDNFKVDIPEGVNDGMRIRVSNKGNIAPNGQRGDLYLQVSVKEDSHFVRHDDDIYFEAPIFFTQVALGGTIKVPSLRGELELEIPKGAKDKQQFTFKGEGVKSVQGYGKGDLIIQIKIEYPKALNNEQKELLEKLQDSFGIESKPHETTFEGMFDKVKKWFS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Finegoldia magna (strain ATCC 29328)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.093 kDa
Sequence
MKNLYEILEVNENATQEEIKKSYRRLAKKYHPDINSGDSEAENKFKEINGAYEVLGDKEKRKKYDMYGDRMFDQGTGGGFSDFGDIFGDFFGDIFGGFSSRSYSKNPNAPRKGSNIQVELEIDFEDSINGTKKEISYKKKVKCHVCNGDGAKPGTEKRQCEKCHGTGIINDTKRTPFGIFTQQSECDKCHGEGYVIDEKCENCKGKGYEIERKTINITIPKGINNGAIMSVKGEGNDGENNGSPGDLYVIIKIREHEFFKRINNDIVFDMPITYAQAVLGSKIEVPTLDGIEEFELPEGTQPNTTFKLKSKGVPYLNSNSRGDILFTVKIIVPKKINKEQKEKLIKFSESMNQELNVNEKKSIFDRIKDMFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.017 kDa
Sequence
MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHRAFDNSSGFSSNFTDFEDLFSNMGSSGFSSFTNIFSDFFGSNKSDYQRSTKGQSVSIDIYLTFKELLFGVDKIIELDLLTNCSACFGSGAESNSDINICNNCHGTGEVLVQKNMGFFQFQQSAKCNVCNGAGKIIKNKCKNCKGKGKYLERKKIEVNIPKGIRPNQQIKLSQKGHASTNNGVNGDLIIDIYLKESKVFEIINNNDILMTYNISYLDSILGNEIIIKTLDGDIKYKLPKSINSNEAIIINNKGLYKSINKDKRGDLIIKVNIVVPKNLTKKEKELIEQIYEQTSFNPENNINQ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma mycoides subsp. mycoides SC (strain PG1)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.961 kDa
Sequence
MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHNAFDGSSGFSSNFADFEDLFSNMGSSGFSSFTNIFSDFFGSNKSDYQRSTKGQSVSVDIYLTFKELLFGVDKIIELDLLTNCSVCFGSGAESNSDISICNNCHGTGEVLIQKNMGFFQFQQSAKCNVCNGAGKIIKNKCKNCKGKGKYLERKKIEVNIPKGIRPNQQIKLSQKGHASINNGVNGDLIIDIYLKESKVFEIVNNNDILMTYNISYLDAILGNEIIIKTLDGDIKYKLPKSINSNEFIIINNKGLYKSINKDKRGDLIIKVNIVVPKNLNKKEKELIEQIYEQTSFNPENNIDQ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.056 kDa
Sequence
MNNTEFYDRLGVSKNASADEIKKAYRKLSKKYHPDINKEPGAEDKYKEVQEAYETLSDDQKRAAYDQYGAAGANGGFGGFNGAGGFGGFEDIFSSFFGGGGSSRNPNAPRQGDDLQYRVNLTFEEAIFGTEKEVKYHREAGCRTCNGSGAKPGTSPVTCGRCHGAGVINVDTQTPLGMMRRQVTCDVCHGRGKEIKYPCTTCHGTGHEKQAHSVHVKIPAGVETGQQIRLAGQGEAGFNGGPYGDLYVVVSVEASDKFEREGTTIFYNLNLNFVQAALGDTVDIPTVHGDVELVIPEGTQTGKKFRLRSKGAPSLRGGAVGDQYVTVNVVTPTGLNDRQKVALKEFAAAGDLKVNPKKKGFFDHIKDAFDGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus clausii (strain KSM-K16)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.795 kDa
Sequence
MSKRDYYEVLGVDRNASVEEVKKAYRKLARKYHPDVNKEEDAEAKFKEVKEAYDTLSDPQKKARYDQFGHADPNQGFGGAGASGDFGGFSDIFDMFFGGGGGRRNPNAPRQGDDLQYTMTLEFKEAVFGKETEIEIPREETCGTCHGSGAKPGTKPDTCSHCGGSGQLNVEQNTPFGRVVNRRVCNYCEGTGKIIKQKCATCSGKGKVRKRKKINIQVPAGIDNGQQLRVAGQGEAGANGGPPGDLYVVFQVKPHEFFERDGEDIYCEVPLTFPQVALGDEIEVPTLTGKVKLKIPAGTQTGTSFRLRGKGVPNVHGRGQGDQHVQVRVVTPKNLTENEKELMREFAGMSGGRPEEQNDGFFDKLRRAFKGD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.435 kDa
Sequence
MAKRDFYEVLGVTKTCTEAEMKVAFRKAAMQWHPDRNPGNEEAEIQFKEINEAYQTLSDGQKRAAYDRYGHAAFEHGGGGNDGFASSMADIFDDLFGDVMGRRGGRNGPARGSDLRYNMEITLEEAFQGKLASLTLPTSITCEACDGTGAKAGAKPRICPTCGGQGRVRAQQGFFAIERTCPQCHGRGEIIDDPCQACGGAGRVTRERTLSVNIPPGVEDGTRIRLAGEGEAGTRGGPAGDLYIFVSTKPHPFFQRDGADLFCRVPISMTQAALGGEVTVHTIDGKEAKVKISEGTQSGKQFKLKNKGMPVLRSREVGDLYIQATVETPQNLTKRQRELLAEFDAESSNKTHPEASGFFARMKDFFENLSGQ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lysinibacillus sphaericus (strain C3-41)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.079 kDa
Sequence
MEKRDYYEVLGLTKSATKDEIKKAYRKLSKQYHPDLNKEPGADEKFKEIAEAYEVLSDDQKKARYDQFGHEDPNAGFGGGFGGGGFGGFEDIFSSFFGGGGRRQDPNAPRKGDDLQYRMNIKFEEAIFGKETEIEIPKDETCETCHGSGAKPGTQPETCSTCNGAGQINQAVDTPFGRMMNRRSCTTCHGTGKIIKEKCSTCRGEGKVQKRKKIKVSIPAGVDDGQQIRVSGQGEPGINGGPAGDLYIMFRVQGHNDFERDGDDIYFELKLTFPQAALGDEIEVPTVHGKVKLRIPAGTQSGAQFRLKDKGVKNVHGYGMGNQYVTVKVMTPEKLTEKQKQLLREFAEISGDIPEEQGSSLFDKIKKKFQGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Macrococcus caseolyticus (strain JCSC5402)
Length
372 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.697 kDa
Sequence
MAKRDYYEVLGLSKGASKEEIKRAYKKLSKKYHPDINKEADAEDKFKEIAEAYEVLSDDQKKAQYDQFGHAGMGQGAGFGGQDFGGFGGFEDIFSSFFGGGARRDPNAPRQGNDLQYQMNVTFEEAVFGAEKEISVKKEVECDTCDGSGAQPGTNIKTCSTCGGRGNVHVEQNTPFGRVRSERTCPDCGGTGKEFEEKCSDCGGTGRKVKTVKISVKVPAGVDTGQQIRLSGQGEPGINGGPAGDLYVVFNVQDHAYFDRSGEDIFYTLELSIAQAALGDEVEVPTLEGKVKLTIPAGTQTGKRFRLKEKGVQNVHGYGRGDEYVTVKVMTPVKMTNRQAELLREFAEIDGHDITEQPSNFFDKTKRFFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus anthracis (strain A0248)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus anthracis
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain AH820)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.404 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPXGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQIIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRNHEFFEREGDHIICEMPLTFAQMALGDEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSQQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain G9842)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.336 kDa
Sequence
MSKRDYYEVLGLSKGASTDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQIIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRNHEFFEREGDHIICEMPLTFAQMALGDEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSQQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain 03BB102)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.349 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain B4264)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.336 kDa
Sequence
MSKRDYYEVLGLSKGASTDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQIIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRNHEFFEREGDHIICEMPLTFAQMALGDEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSQQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain AH187)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQIIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRNHEFFEREGDHIICEMPLTFAQMALGDEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSQQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain Q1)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQIIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRNHEFFEREGDHIICEMPLTFAQMALGDEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSQQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.465 kDa
Sequence
MSKRDYYEVLGLSKGASTDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQIIKEKCTTCHGSSKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPARDLYVVVHVRNHEFFEREGDHIICEMPLTFAQMALGDEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSQQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cereus (strain ZK / E33L)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.349 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.363 kDa
Sequence
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.021 kDa
Sequence
MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVGAGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRGGFGGGRRSGSQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCGDCNGSGAAKGSSPTTCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTTISNPCKTCGGQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGSHGDLYVVTHIKRHELFERQGNDLILVRKITLAQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGMPYLGAYGKGDQHVVVKIEIPKKITRRQRELIEAFARESGENIPGSKGKIFTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.021 kDa
Sequence
MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVGAGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRGGFGGGRRSGSQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCGDCNGSGAAKGSSPTTCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTTISNPCKTCGGQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGSHGDLYVVTHIKRHELFERQGNDLILVRKITLAQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGMPYLGAYGKGDQHVVVKIEIPKKITRRQRELIEAFARESGENIPGSKGKIFTK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Francisella tularensis subsp. holarctica (strain LVS)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.481 kDa
Sequence
MQQKCYYEILNISKTASGVEIKRAYRKLAMKYHPDRNPGDKEAEIKFKEISEAYEILSDDSKRSRYDQFGHAGVNQQSGFGGTGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTLEITLEEAFFGVEKEITIPRMESCDSCDGTGSKSRSKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGYSITDPCDACYGNGKVKKQKTLKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYVQIIIKEHKIFERRDINLYCEMPISFTKACLGGDIKVPTLDGEVVLKVVPETQTGKVFRLREKGMKSLRGHRRGDLLCKVVVETPVNLSAEQKELLEKFADSLGEDYQSKHAPKSKTWFDNVKDYAKKFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Francisella tularensis
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.481 kDa
Sequence
MQQKCYYEILNISKTASGVEIKRAYRKLAMKYHPDRNPGDKEAEIKFKEISEAYEILSDDSKRSRYDQFGHAGVNQQSGFGGTGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTLEITLEEAFFGVEKEITIPRMESCDSCDGTGSKSRSKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGYSITDPCDACYGNGKVKKQKTLKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYVQIIIKEHKIFERRDINLYCEMPISFTKACLGGDIKVPTLDGEVVLKVVPETQTGKVFRLREKGMKSLRGHRRGDLLCKVVVETPVNLSAEQKELLEKFADSLGEDYQSKHAPKSKTWFDNVKDYAKKFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Francisella tularensis subsp. tularensis (strain WY96-3418)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.468 kDa
Sequence
MQQKCYYEILNVSKTASGVEIKRAYRKLAMEYHPDRNPGDKEAEIKFKEISEAYEILSDDSKRSRYDQFGHAGVNQQSGFGGTGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTLEITLEEAFFGVEKEITIPRMESCDSCDGTGSKSRSKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGYSITDPCDACYGNGKVKKQKTLKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYVQIIIKEHKIFERRDINLYCEMPISFTKACIGGDIKVPTLDGEVVLKVVPETQTGKVFRLREKGMKSLRGHRRGDLLCKVVVETPVNLSAEQKELLEKFADSLGEDYQSKHAPKSKTWFDNVKDYAKKFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia akari (strain Hartford)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.036 kDa
Sequence
MSQDYYKILGVSKTASQADLKKAYLKLAKQYHPDTTDDKDAEKKFKEINRAYDVLKDEQKRAAYDRFGHDTFQNQQSRGGGGSHAGFHHDINDIFGDFFSDFMGGGRRKPTSSKARGSDLKYDLTINLEEAFHGIEKNISFSSEVKCDTCHGSGSEKGETVTTCDACGGVGATRIQQGFFTIEQACHKCKGNGQIIKNPCKKCHGMGRCHKQRNLSVNIPAGVENGTRIRHTGEGEAGIRGGNSGDLYVDIAITPHDIYKVDGANLHCKLPISFVNAALGGEIEVPVIEGRKVNLTIPAGTQNGDQLRLRSKGMPKMRSTIRGDMITHIHIEVPKNLSKRQCELLEEFKKESISEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.027 kDa
Sequence
MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINSAYDVLKDEQKRAAYDRFGHDTFQYQQSRGGGGNHGGFHPDINDIFGDFFSDFMGGGRRKPTSSKARGSDLKYDLTINLEEAFHGIEKNISFSSEVKCDTCHGTGSEKGETVTTCDACGGVGATRIQQGFFTIEQACHKCQGNGQIIKNPCKKCHGMGRYHKQRNLSVNIPAGVENATRIRHPGEGEAGIRGGNSGDLYVDIAIKPHDIYKVDGANLHCKLPISFVNAALGGEIEVPIIEGGKVNLTIPAGTQNGDQLRLRSKGMSKMRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDGSFFNKMKSLWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Methylovorus sp. (strain SS1 / DSM 11726)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.052 kDa
Sequence
MAKKDYYEVLGVNRDASDEEIKKSYRKLAMKYHPDRNPDNPKAEESFKEAKEAYEVLSDEQKRAAYDQYGHAGVDPSAGPGPRQGFGNFADAFGDIFGDIFGGGGGNRRSNVYRGADLRYNMEISLEDAARRTETKIRIPVMSECETCHGSGARPGTQPVTCTTCGGHGQVRMQQGFFSVQQTCPKCHGSGKMVKEPCPSCQGAGRVKKHKTLSVKIPAGVDEGDRIRLSGEGERVNGGPPRDLYVVVHLKQHDIFQRDGGNLHCEMPISFTTAALGGEIEIPTLDGHAKMKIPPETQTGATFRLRGKGIKPLRTNDPGDLMCHVVVETPIKLTERQKELLREMEEINLQDSDKHSPRAKGWMDKVKDFFQ

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.776 kDa
Sequence
MAGKRDYYEILGVEKGADQDTIKKAYRKLAMQFHPDKNPGNKEAEEKFKEAAGAYEVLSDAQKRAQYDRFGHDAFTRGGGGGGFTDAEDIFSHFGDIFGDFFGGGMGGQQRQRRNRNEPRRGSDLRYVTEITLKDVITGIEKEIEFDTDKNCDECKGTGAEKGSQVSTCGTCGGSGQVVRQQGFFAMASTCPTCHGQGTVIKNPCKPCKGKGRVAEHRKIRLNIPAGVDTGTRLRVATEGEGGYMGGPPGDLYVEIRVKQHNNFERRNEDLFAELSLPYVQMLLGAEIEVPTVTGKAKLEVPKGTHHGDNVKLVGEGLPSLRGNRRGDIYFTVNVQFPEKLHKDEEKLLREIAKARGLNVTSEGGFFGKKK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.855 kDa
Sequence
MSKKDYYEILGIAKNANEQDIKDAYKRLAKKYHPDRNKDKDAETKFKEMKEAYEVLSDQQKRAAYDQHGHTAFEQSGMGGGFHNSSNFSNVFNDVFSDFFGGHQQRTQRGRDLRYTLNLTLEEAVRGASKEIHITTLVHCEHCKGSGAKQGTRPVTCTTCRGVGEVHMQQGFFTIQQTCPRCHGQGQMIKDPCRQCRGQGKVEEPKTFSVKVPAGIDSNDCLRLNGKGEVGEMGAPSGDLYVQIHVDRHHIFERSKNNLYCKVPINFTTAALGGEIEVPTLDGAIKLKIPPETQTGQCFRIPNKGIKPEKKTPGDLFCTVFIETPVHLNEKQKKLLRDLDQSFCETSSKKNTPETKKFLESMKKFFDNLTH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)
Length
371 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.945 kDa
Sequence
MNNTEFYDRLGVSKDASQDEIKKAYRRMSKKYHPDINKEAGAEEKYKEVQEAYETLSDTQKRAAYDQYGAAGANGGFGGFDGGGFGGFEDIFSSFFGGGGMRNPNAPRQGDDLQYRVNLSFEEAIFGAEKEVSYNRESSCHTCSGSGAKPGTSPVTCQKCHGSGVINVDTQTPLGTMRRQVTCDVCQGSGQEIKEKCPTCHGTGHEKKTHKVSVKIPAGVETGQQIRLTGQGEAGFNGGPYGDLFVIINVLPSQQFERNGSTIYYTLNISFVQAALGDTIDIPTVHGAVEMSIPAGTQTGKTFRLRGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQKEALHAFAEASGDKMVHPKKKGFFDKVKDALDVD

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Length
370 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.58 kDa
Sequence
MSKRDYYEVLGVDRNASADEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAFDTLSDPQKKAHYDQFGHTDPNQGFGGGGAGDFGGFSDIFDMFFGGGGGRRNPNAPRQGADLQYTMTLEFKEAVFGKETTIEIPREETCHTCSGSGAKPGTKPESCPHCGGSGQLNIEQNTPFGRVVNRRVCHHCEGTGKYIKHKCATCGGKGKVRKRKKINVKVPAGIDHGQQIRLSGQGEAGVNGGPAGDLYIVFNVKPHEFFERDGDDIYCEMPLTFVQVALGDEIEVPTLNGKVKLKIPAGTQTGTSFRLRGKGVPNVHGRGQGDQHVQVRVITPKQLSEKEKELLREFAQMSGGRPDEQDDSFFAKVKRAFKG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
Length
370 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.396 kDa
Sequence
MKREKKDYYEILGVPRNATQEEIRKAYKRLVKEWHPDRHPENRKEAEQRFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPVYQEAETGGSFFEDVFREFENIFNRDIFDVFFGEESGRRERREYARRGEDIRYTIEVNLSDLINGTEIPIEYERYETCPRCGGTGVEPDSGYISCPRCGGTGRIREEKRSFFGYFVSERTCDECGGTGRVPQELCHECGGSGRVLRRVRRTIKIPPNIEDGGHLRIPGGGNAGYYGGPYGDLIITVRVRSDSRFKRSGKDLIYDITIDYLQAILGTTVEIPLPEGGTTMLKIPPGTQPETVFRLKGKGLPGEYGRRGDLLVNVHVEIPKNLSREERKVLEDLAKKRGIPVA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia prowazekii (strain Madrid E)
Length
370 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.013 kDa
Sequence
MSQDYYQVLGVSKTASQADIKKAYLKLAKQYHPDTTNANDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQSQQARGGGNNGSFHPDINDIFGDFFSDFMGSGRRKQTSSKIRGSDLKYDLTIKLEEAFHGIEKNISFSSEVKCDTCHGTGSEKGETITTCDACGGVGATRIQQGFFTLEQTCHKCQGNGQIIKNPCKKCHGMGRYHKQRNLSINIPAGVENGTRIRHTGEGEAGIRGGNNGDLYVDIAIKPHDIYKVDGANLHCKLPISFVHAALGGEIEVPVIEGGKVKLTIPAGTQNGDQLRLRSKGMSKVRSTIRGDMLTHIHVEVPKNLSKKQRELLEEFKKESINEKENDSSFFNKMKSMWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Length
370 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.145 kDa
Sequence
MSQDYYQVLGVSKTASQADIKKAYLKLAKQYHPDTTNAHDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQARGGGNNSGFHHDINDIFGDFFSDFMGSGRRKQTSSKIRGSDLKYDLTIKLEEAFHGIEKNISFSSEVKCDACHGTGSEKGETVTTCDSCGGVGVTRIQQGFFTLEQTCHKCQGNGQIIKNPCKKCHGMGRYHKQRNLSINIPAGVENGTRIRHSGEGEAGIRGGNNGDLYVDIAIKPHDIYKIDGANLHCKLPISFVHAALGGEIEVPVIEGGKVKLTIPAGTQNGDQLRLRSKGMSKIRSTIRGDMLTHIHVEVPKNLSKRQRELLEEFKKESINEKENDSSFFNKMKSMWS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Roseiflexus castenholzii (strain DSM 13941 / HLO8)
Length
370 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.839 kDa
Sequence
MAVKRDYYEVLGVQRNASQDEIKKAFRRLARQYHPDVNKAPDAEAKFKEINEAYEVLSDPEKRSMYDRFGHAGPTAAPGFDPFASADPFSSIFETFFGGTMRGTQRGPQRGADLRYTLSISFEEAIFGVEKTIEYRRMETCPACRGSGAEPGTEPVRCPKCGGLGEIRQRAPLFNMVTVTTCDMCRGEGTVIAIPCRECRGEGRIRQTRKITVRVPPGVDSSAQIRISGEGDAGPRGGPYGNLYVVIDVQPHPFFIREGNDIILELPLNVAQAALGTEVDVPTIEGTERLHIPPGVQNGAVFRIRGKGAPFLRSSGRGDQIVVVRVVVPTNLNDHQRRLFEELARSLENEPIGNQRDEGFFGRIKNALGL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Roseiflexus sp. (strain RS-1)
Length
370 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.795 kDa
Sequence
MAVKRDYYEVLGVQRNASQDEIKKAFRRLARQYHPDVNKAPDAEAKFKEINEAYEVLSDPEKRSMYDRFGHAGPTAAPGFDPFSSADPFSSIFETFFGGTMRGSQRGPQRGADLRYTLSISFEEAVFGVEKTIEFRRLETCPACRGSGAEPGTEPVRCPKCGGLGEIRQRAPLFNMVTVTTCDMCRGEGTVIAIPCRECRGEGRVRQTRKITVRVPPGVDNSSQIRISGEGDAGPRGGPYGNLYVVIDVQPHPYFIREGNDIILELPLNVAQAALGVEVEVPTIDGTEHLRIPPGVQSGAVFRIRGKGVPFLRSSGRGDQIVVVRVVIPTNLTDHQRRLFEELARSLEKEPIGGQRDEGFFGRIKNALGL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.646 kDa
Sequence
MADHYEVLGVERNATPDEIKKAYRRLARELHPDVNPSTEAQERFKLVTHAYDVLSDPQQRQQYDRGGASGFGGGGGADFSGFGDIFETFFGGGGASRGPRSRRERGQDALLRVEVDLDEVVFGAHRDLEVDTAIVCETCDGSCCQPGTAPVPCDICHGTGSIQRSVRSLLGNVMTSSPCGSCRGYGTVIATPCVTCQGQGRVRARRTVPVDIPAGVDTGLRLQMPGSGEAGPAGGPNGDLYLEIKVKHHDVFSRDGDDLLCTLEVSMADAILGAAATIKALDGDIRLELKPGTQSADIVSVKDRGITHLRCSGRGDLRVGIQVVTPTKLDHREKELIKKFAESHKASEPSLARFQQGLFAKLRDRFLNV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.358 kDa
Sequence
MKKEKKDYYEILGVPRDATQEEIKRAYKRLVKEWHPDRHPENRKEAEQRFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPTYQETESGGFFDDIFRDFENIFNRDIFDVFFGERPHQEERREYARRGEDIRYEIEVTLSDLINGAEIPVEYERYETCPRCGGTGVEPNAGYMDCPSCGGTGRIREERRSFFGYFVSERTCERCGGTGKIPREYCHECGGSGRVLRKVRRTVKIPPNVEDGTHLRITGGGNAGYYGGPYGDLIIIVRVKPDPRFKKSGSDLVYDVTIDYLQAILGTTVEVPLPEGGTTMLKIPPGTQPETVFRLKGKGLPNRYGRRGDLIVNVHVEIPKSLSREERKVLEELAKKRGVTIG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.236 kDa
Sequence
MKREKKDYYEILGVPRDATQEEIKRAYKRLVKEWHPDRHPENRKEAEQRFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPTYQETESGGFFEDIFKEFENIFNRDIFDVFFGERPGQEEKREYARRGEDIRYEIEVTLSDLINGAEIPVEYERYETCPRCGGTGVEPNAGYINCPSCGGTGRIREERRSFFGYFVSERTCERCGGTGKIPREYCHECGGSGRVLRKVRRTVKIPPNVEDGTQLRITGGGNAGYYGGPYGDLIVIVRVKPDPRFKKSGSDLVYDVTIDYLQAILGTTVEVPLPEGGTTMLKIPPGTQPETVFRLKGKGLPNRYGRRGDLIVNVHVEIPKTLSREERKVLEDLAKKRGVTIG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermotoga sp. (strain RQ2)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
42.374 kDa
Sequence
MKKEKKDYYEILGVPRDATQEEIKRAYKRLVKEWHPDRHPENRKEAEQRFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPTYQETESGGFFDDIFREFENIFNRDIFDVFFGERPHQEERREYARRGEDIRYEIEVTLSDLINGAEIPVEYERYETCPRCGGTGVEPNAGYINCPSCGGTGRIREERRSFFGYFVSERTCERCGGTGKIPREYCHECGGSGRVLRKVRKTVKIPPNVEDGTQLRITGGGNAGYYGGPYGDLIVIVRVKPDPRFKKSGSDLVYDITIDYLQAILGTTVEVPLPEGGTTMLKIPPGTQPETVFRLKGKGLPNRYGRRGDLIVNVHVEIPKSLSREERKVLEELAKKRGVTID

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Nitrosomonas eutropha (strain DSM 101675 / C91)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.052 kDa
Sequence
MSQRDYYEVLGVGRDADESELKKVYRKLAMKYHPDRNAGDAKAEERFKEIKEAYEVLSDSNKRAAYDQFGHAGLNGGVGGAGAQGFSDAFSDIFSDLFGMRGGGRSSVHRGADLRYNLEITLEQAARGTETKIRIPRQEACDTCHGSGAKPGTSPKTCPTCNGHGQVRMQQGFFSIQQTCSHCHGSGKIVSDPCTDCQGAGRVKRHKTLSVRIPAGVDEGDSIRLTGEGEAGASGGLAGDLYVVIHLASHPVFQREGNHLHCEIPISFTVAALGGEIEVPTLDGHARIKVPTGTQTGKIFRLRSKGITGVRNQSTGDLLCHVAVETPVNLTPRQKELLEEFESISQKDGSLHHPRAKSWMEKAREFFTE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.042 kDa
Sequence
MSQSDYYEVLGVGRDADENELKKAYRKLAMKYHPDRNAGDTKAEERFKNIKEAYEILSDPNKRAAYDQFGHAGLNGGMGGAGAQGFSDAFSDIFSDLFGMRGGGRSSVHRGADLRYNLEITLEQAARGAETQIRIPRQEVCDTCHGSGAKPGTSPKTCPTCNGHGQIRMQQGFFSIQQTCSHCQGSGKVVSDPCGDCHGAGWVKRQKTLSVRIPAGVDEGDSIRLTGEGEAGANGGQAGDLYIVIHLASHPVFQREGNHLHCEIPISFTVAALGGEIEVPTLDGHARIKVPAGTQTGKIFRLRSKGITGVRNQSTGDLLCHVAVETPVDLTARQKELLEEFESISQKDGSRHHPRAKSWMEKAREFFAE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Helicobacter pylori (strain J99 / ATCC 700824)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.85 kDa
Sequence
MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLGDEKKRALYDRYGKKGLNQAGTSQSDFSDFFEDLGSFFEDAFGFGARGSKRQKSSIAPDYLQMIELSFKEAVFGCKKTIKAQYQSVCESCDGTGAKDKALENCKQCNGQGQVFMRQGFMSFAQTCGACQGKGKIIKTPCQACKGKTYILKDEEIDAIIPEGIDDQNRMVLKNKGNEYEKGKRGDLYLEARVKEDEHFKREGCDLFIKAPVFFTTIALGHTIKVPSLRGDELELKIPRNAKDRQAFAFRNEGVKHPESSYRGSLIVELQVIYPKSLNKEQQGLLEKLHASFGYEGEPHKSVLETCVSKIKDWFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Helicobacter pylori (strain ATCC 700392 / 26695)
Length
369 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.851 kDa
Sequence
MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQGDFSDFFEDLGSFFEDAFGFGARGSKRQKSSIAPDYLQTLELSFKEAVFGCKKTIKVQYQSVCESCDGTGAKDKALETCKQCNGQGQVFMRQGFMSFAQTCGACQGKGKIVKTPCQACKGKTYILKDEEIDAIIPEGIDDQNRMVLKNKGNEYEKGKRGDLYLEAQVKEDEHFKREGCDLFIKAPVFFTTIALGHTIKVPSLKGDELELKIPRNARDKQTFAFRNEGVKHPESSYRGSLIVELQVIYPKSLNKEQQELLEKLHASFGYEGEPHKSVLETCISKIKDWFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Peanut witches'-broom phytoplasma
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.915 kDa
Sequence
MKQKKDYYEVLELSRDAKLDDIKKAYRRLSKKYHPDVCKEANADAKFKEVQEAFDVLSNTNKRAQYDQMGHNFNNQGFNSDFQGFQSANFEEFEDLFSSFFGRRKSNRHQEDIKGEDHHIKLTISFMESVLGTQKTVTFNVKENCEKCDGTGAKTKNDIRICNVCKGNGYISYTQQGWFVSVFGKQICPECGGNKKIYFRPECKFCKGVGMVKSEHKVTLNIPAGVESGMRLKSPNQGHQGPSGAPNGDLYVDINVQPHKTFQRKGNDIFSSILINFYQAALGTIINVDTIHGNVQLKIPAGTQTDTKFRLKNKGVPYVNSPFSIGDHYVIVKIYTPQNLSNTQKKLFEQLEELEELNRKSKTNSSWF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xylella fastidiosa (strain M23)
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.418 kDa
Sequence
MSKRDYYQVLGVPRTASEDDLKKAYRRCAMKYHPDRNPGDAAAEAAFKECKEAYEVLADTKKRKLYDTHGHAAFEHGVGSGNTPDMNDIFGDIFGNIFGGARASRRGADVGYMVELDLEEAVAGVERQIQIPTLVECTHCHGSGSEDGHVETCGTCRGSGQVRIQRGIFAMQQTCPHCGGRGVIIRNPCKVCNGAGRVEDHKTLSVKIPAGVDNGDRIRLSGEGEQGPDGVPPGDLYVEVRVREHPIFQRDGDDLHCEVPVRISQAALGDIVRVATLDGEAEIRIPAETQSGKLFRLRGKGVRSVRSRTEGDLYCRIVVETPVNLTAEQRKLLEQFEMTFAGEDARKHSPKSATFLDGVKSFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xylella fastidiosa (strain 9a5c)
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.372 kDa
Sequence
MSKRDYYQVLGVPRTASEDDLKKAYRRCAMKYHPDRNPGDAAAEAAFKECKEAYEVLADTKKRKLYDTHGHAAFEHGVGGGNAPDMNDIFGDIFGNIFGGARASRRGADVGYMVELDLEEAVAGVERQIQIPTLVECTHCHGSGSEDGHVETCGTCRGSGQVRIQRGIFAMQQTCPHCGGRGVIIRNPCKVCNGAGRVEDHKTLSVKIPAGVDNGDRIRLSGEGEQGPEGVPPGDLYVEVRVREHPIFQRDGDDLHCEVPVRISQAALGDIVRVATLDGEAEIRIPAETQSGKLFRLRGKGVRSVRSRTEGDLYCRIVVETPVNLTAEQRKLLEQFEMTFAGEDARKHSPKSATFLDGVKSFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xylella fastidiosa (strain M12)
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.335 kDa
Sequence
MSKRDYYQVLGVPRTASEDDLKKAYRRCAMKYHPDRNPGDAAAEAAFKECKEAYEVLADTKKRKLYDTHGHAAFEHGVGGGNAPDMNDIFGDIFGNIFGGARASRRGADVGYMVELDLEEAVAGVERQIQIPTLVECTHCNGSGSEDGHVETCGTCRGSGQVRIQRGIFAMQQTCPHCGGRGVIIRNPCKVCNGAGRVEDHKTLSVKIPAGVDNGDRIRLSGEGEQGPDGVPPGDLYVEVRVREHPIFQRDGDDLHCEVPVRISQAALGDIVRVATLDGEAEIRIPAETQSGKLFRLRGKGVRSVRSRTEGDLYCRIVVETPVNLTAEQRKLLEQFEMTFAGEDARKHSPKSATFLDGVKSFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.418 kDa
Sequence
MSKRDYYQVLGVPRTASEDDLKKAYRRCAMKYHPDRNPGDAAAEAAFKECKEAYEVLADTKKRKLYDTHGHAAFEHGVGSGNTPDMNDIFGDIFGNIFGGARASRRGADVGYMVELDLEEAVAGVERQIQIPTLVECTHCHGSGSEDGHVETCGTCRGSGQVRIQRGIFAMQQTCPHCGGRGVIIRNPCKVCNGAGRVEDHKTLSVKIPAGVDNGDRIRLSGEGEQGPDGVPPGDLYVEVRVREHPIFQRDGDDLHCEVPVRISQAALGDIVRVATLDGEAEIRIPAETQSGKLFRLRGKGVRSVRSRTEGDLYCRIVVETPVNLTAEQRKLLEQFEMTFAGEDARKHSPKSATFLDGVKSFWDRMTS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Mycoplasma hyopneumoniae (strain 232)
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.871 kDa
Sequence
MAKQDFYKILGVEKSASLTEIKKAYRNLVNIYHPDKNTKKSAEEQKQAEAKFKEIQEAYEILSDETKRKQYDKFGHAAFDQQFGGGSSGFSGFDFGDIFSSFTSGFGFGGSQEQKYSRPLKGENFQAKIYISFIESILGKEISQKLTKYDQCDNCKGSGANSSSDITTCYNCQGRGMQTEVLNIPGFGRVQNKTTCSVCLGSGKNITKNCKKCRGKTIVETKEEVTIKIPAGIQDGMFIRVAGFGGPGHKGGPSGDLHLEINVRQHKHFTRSGNDIHVNMPVSIIDVINQNTVEVPSPTGLKKVRLYDYYKSGQIVNVLRAGAPDPKNPRIIGDLKVHLIFYIPEFSPRQKDDLNQVFAQINDKTKAK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus weihenstephanensis (strain KBAB4)
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.251 kDa
Sequence
MNKRDYYEVLGLSQGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACGHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRNHEFFEREGDHIICEMPITFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFRKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Lysinibacillus sphaericus
Length
368 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.692 kDa
Sequence
MEKRDYYEVLGLTKDEIKKAYRKLSKQYHPDLNKEPGADEKFKEIAEAYEVLSDDQKKARYDQFGHEDPNAGFGGGFGGGGFGGFEDIFSSFFGGGGRRQDPNAPRKGDDLQYRMNIKFEEAIFGKETEIEIPKDETCETCHGSGAKPGTQPETCSTCNGAGQINQAVDTPFGRMMNRRSCTTCHGTGKIIKEKCSTCRGEGKVQKRKKIKVSIPAGVDDGQQIRVSGQGEPGINGGPAGDLYIMFRVQGHNDFERDGDDIYFELKLTFPQAALGDEIEVPTVHGKVKLRIPAGTQSGAQFRLKDKGVKNVHGYGMGNQYVTVKVMTPEKLTEKQKQLLREFAEISGDIPEEQGSSLFDKIKKKFQGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Length
366 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.135 kDa
Sequence
MSKRDYYEVLGVSKSASKDEIKKAYRRLAKKYHPDVSKEENAVEKFKEVQEAYEVLSDEQKRAQYDQFGHAGSSQGFGGGDFGGGFGFEDIFSSFFGGGSRRRDPNAPRQGADLQYQVTLEFEEAIFGKELNVEIPVEDPCDTCHGSGAKPGTTKETCKYCSGTGQISVEQNTPFGRIVNRQTCRHCSGTGQMIKEKCTTCHGTGKVRKRKKINVKIPAGIDNGQQIRVAGKGEAGVNGGPAGDLYVVVHVREHEFFERDGDHIICEMPLTFAQAALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTNLTAHQKELLREFAGQEDKDDSLFGKLKRAFKGE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Length
365 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.584 kDa
Sequence
MAKDYYKILGVDRNATDEEIKKAFRELAKKWHPDLHPENKQEAEEKFKEISEAYEVLSDPQKRRMYDQTGTVDFGAGGQNFNWDNFTHYSDLNDIFNDIFGGNFASDFFSGFGRGQREEQYDLDLYTNLDITLEDAYYGTEKRIKYRRNAMCPDCNGTGAKNGKLITCPTCNGTGQQRIVRGQGFFRMVTVTTCQTCGGRGRIPEEKCPRCNGTGTVVVNEDISVKIPKGATDNLRLRVQGKGQSYNGRTGDLYVVLRVRNDRNVQRINDDLMIDQKINFAQAALGDTIEVNLFREKYSLKIPEGTQPGEVLRIKGAGMPHLNGHGSGDLLVRVNVEVPKRLTQKQKDLIREIFDIKENHRSWFH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Length
365 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
41.149 kDa
Sequence
MAKDYYKILGVDRNASEEDIKKAFRELAKKWHPDLHPDNKAEAEEKFKEISEAYEVLSDPEKRRIYDQTGSVDFGGGGSNFNWDNFTHFSDINDIFNEIFGGNFGSDFFSGFGNRQSTRNIDLDMYTNLDISLEEAYYGTEKRIKFRRNAICPDCKGTGAKNGKLITCPTCHGTGQQRVVRGQGFFRMVTVTTCNTCGGKGRIPEEKCPRCNGTGTIVVDEDITVKIPRGATDNLRLRVSGKGQSYDGRTGDLYVILRIKQDKNLQRINDDLLLDQKINFGQAALGADIPIQIFNEKYNLKIPEGTQPGDVIKIKGAGMPHLNGHGSGDLLVRINVEVPKRLTAKQRELIRELFDIKENHKSWFH

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA)
Length
365 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.632 kDa
Sequence
MSQRDFYEILGIAKNTDVKQIKKAYKRLAMKHHPDRVKDNKELAEKKFKEIQKAYAILSDTQKRQAYDQFGHAGINGNAGATSGTSFSSSGFGDIFGDIFGGGSQQSNNRGSDLRYDLEIDLKEAAQGTTVKIRIPKNETCDTCSGTGAKPGTSVKTCLTCGGAGQIQIQQGFFAVQRPCNACSGTGQRIESTCNNCHGKGVVHKQKTLSVKIPAGVDTGNRIRLSGEGEAGIRGGLSGDLYVQIHVKKHAIFERQDSDLYCEVPIDFATAVLGGQVEVPTLDNKLNIKVPAGTQTGKLFRLRSKGITHLQHGGSGDVICKVKLETPINLSKKQQDLLQKFSNSCGKKHHPESNSFFGKMKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA)
Length
365 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.632 kDa
Sequence
MSQRDFYEILGIAKNTDVKQIKKAYKRLAMKHHPDRVKDNKELAEKKFKEIQKAYAILSDTQKRQAYDQFGHAGINGNAGATSGTSFSSSGFGDIFGDIFGGGSQQSNNRGSDLRYDLEIDLKEAAQGTTVKIRIPKNETCDTCSGTGAKPGTSVKTCLTCGGAGQIQIQQGFFAVQRPCNACSGTGQRIESTCNNCHGKGVVHKQKTLSVKIPAGVDTGNRIRLSGEGEAGIRGGLSGDLYVQIHVKKHAIFERQDSDLYCEVPIDFATAVLGGQVEVPTLDNKLNIKVPAGTQTGKLFRLRSKGITHLQHGGSGDVICKVKLETPINLSKKQQDLLQKFSNSCGKKHHPESNSFFGKMKSFFE

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Borreliella bavariensis (strain ATCC BAA-2496 / DSM 23469 / PBi)
Length
364 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.612 kDa
Sequence
MKKDYYEILGLSKGASKDEIKKAYRKIAIKYHPDRNQGNEEAASIFKEATQAYEVLIDDNKKAKYDRFGHSAFEGGGFEGFSGGFSGFSDIFEDFGDIFDSFFTGNKGQERNRKHARGEDLGYNIEISLENAYFGYKNNINITRQILCHSCLGKKSEKGTSPSICNMCNGSGRVVQGGGFFRVTTTCSKCYGEGKTISNPCKSCKGKGRITNQETIQLNIPSGIDNNQQIKMKGKGNVNPDNQEYGDLYVKILIRSHKIFKRNGKDLYAMLPISFTQAALGKEVRIKTIASKEIKIQIPKGIENEEQIIVKGAGMPILQTEKFGNLILITKIKTPKNLNSNAIKLFENLSKELRDGDEIDLLKV

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Length
364 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.498 kDa
Sequence
MKKDYYEILGLSKGASKDEIKKAYRKIAIKYHPDRNQGNEEAASIFKEATQAYEILIDDNKKAKYDRFGHSAFEGGGFEGFSGGFSGFSDIFEDFGDIFDSFFTGNKGQERNRKHAKGEDLGYNIEISLENAYFGYKNNINITRQMLCDSCLGKKSEKGTSPSICNMCNGSGRVVQGGGFFRVTTTCSKCYGEGKIISNPCKSCKGKGSLTKQETIQLNIPPGIDNNQQIKMKGKGNVNPDNQEYGDLYVKILIRSHKVFKRNGKDLYAMLPISFTQAALGKEVKIKTIASKEIKIHIPKGINNEEQILIKNAGMPILQTEKFGNLILITKIKTPKNLNSNAIKLFENLGKELKDGDEIDLLKA

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Ruthia magnifica subsp. Calyptogena magnifica
Length
364 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.383 kDa
Sequence
MSQKDYYEILGVAKNADAKQIKKAYKRLAMKHHPDRVKNDKASAEKKFKEIQKAYAILSDVQKRQAYDQFGHVGGNANVGSAGGNPFGGGFGDIFGDIFGGGSQQSNNRGSDLRYDLEIDLKKAAQGSTVKIRIPKNETCDTCSGIGAKSGTNVKTCSICSGVGQVQTQQGFFTVQRPCGTCSGTGQKIEFPCGTCRGQGLVRKQKTLSVKIPAGVDTGNRIRLSGEGEAGTIGSSSGDLYVQVHVKKHAIFEREDNDLYCEVPIDFATAALGGSIEVPTLENKLKIKVPSGTQTGKLFRLRDKGISHLQRDGSGDLICQVKIETPVNLNKKQQDLLQKFSSSCGKKHHPESDSFFDKMKSFFG

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
Length
359 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.379 kDa
Sequence
MSDYYEILGVPKDADSDEIKKAFRKLALKYHPDRNAGDKEAEEKFKEINEAYQVLGNDERRQTYDRYGKEGLNGAFGNDFGGFDFGDIFDTFFGGGGFNKSRSQRYDDAYDLDSEILVSISFKDAFFGVSKDIKYKIKKPCKTCDGTGSKDKKLNTCPYCGGSGKIVKRSGFLSFAQTCPFCKGSGQIVKEKCHDCAGKGFIEEQVNVKFDIPKGVNTGIRIRIAKKGNISKSGEIGDLYVAVQVKDDKFFVRSADDIYIEVPVFFTQAILGKTIKVPTMHGEKELQLKVGSKDKDQFVIEKEGFENIRTKIAGNLIVQINVQTPKKLTDEQIELLEKLHESFDKTADGIFDKIKNWFK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Length
357 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
40.043 kDa
Sequence
MAKDYYAILGVDRNASQDDIKKAFRELAKKYHPDANPGNKEAEEKFKEIAEAYEVLSDPQKRKQYDETGTTDFNAGSGFNWQDFTHFDDINDIFNQFFGGNFGDTFFGGYTNQPDLDIYLRVNISLEDAYYGASKNVKYRRNAMCEHCSGTGAENKVLITCPTCHGSGQERITRGQGFFRMVTVTECRTCHGRGKIPQKPCTVCHGTGTVSKNEDISVNIPKGADTNLKLRLKNMGNSYGGVTGDLYIVLIVNNPPGIRRSGQDIYVEHTIDFPEAALGGEEEIKLFRESYNLKIPAGTQPGEILKIKGAGMPRINGHGSGDLNVIIKIEVPKHLTSRQKELLEEFRNEKKKSWFHF

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
Length
356 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
39.872 kDa
Sequence
MPIKDYYQILGVSKDATAEEIKKAYRRLAKEYHPDISADENASEKFKEINEAYHILSDEERRKEYDRILKSGDEKSYRDFMEYIQDFLESIWQGMRRSPKPKKGGDVRLKLELTLEEAAFGCEKDIEYERWIDCPTCEGKGYVGKMEKVTCHACEGTGRRVSGIFSFPRPCSVCKGRGFIIKNQCPACSGRGRVAMHSLLRVNVPPGTDEGDVLKVPGKGHTGERGGEAGDLYLRVSLKPHPIFKKVGKDLYMEAFISFPLAVLGGTTKIKTLEGSYQEVFLQPGTECGSTKRLQGLGYPIAGGRGDLIITFRIEVPKNVNSNIRALIEKLAKELGEEGIEYQSGVITKILSLLKL

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Length
350 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
38.926 kDa
Sequence
MKDYYAILGVSREASQEEIKKAYRRLALKYHPDRNPGDKEAEERFKEINEAYAVLSDPKKRAAYDRGHLEAPEYRPEDLFDLFFQEVFGVRGHRRPPRGEDLEAEVEVELQDLLHGAEKEVRYTRLVPCEACGGEGGRRTPCPTCRGQGVVESYRQSFFGTVVTRTACPHCKGRGYLLAETCPACRGRGRVPREERVRVQVPPGMDEGHLLRVPGYGNLGPGGPGDLYLRIRVRPHPHLERQGPDLVYRLRLGLAQAALGARVVVPGLEGPIPLDIPPGTGHGEVFALEGGGLPLPGGRGRGTLRVVVELAVPKKLSPKAQKLLRAYAEEVGEEVAPEGFWERLKGFFRK

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Tropheryma whipplei (strain TW08/27)
Length
348 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
38.521 kDa
Sequence
MEDLYGILGVDHDASVDEIRRAYRRLARELHPDINPDSADRFKAVTHAYNILSDPEQRQRYDRHVSGGFSSDFNLSDLFQSFFDTSAEFQRGSDLLVNIDIDLKTAIYGGSQVVKIDSLVVCDVCNGTRSEPGYKAEVCFDCNGSGVVRGEVRTTLGNLITQNTCSKCRGNGERIDHPCRRCYGNGSRSAPRDITINIPPGVETGMRIKIPNMGNAGGAMPGDLYVDCKVKEHPYFLRDGQDLYCRLDISLVDALLGTKVKIDSLDGELAVVIPALSQNRDVIRIANKGAVTLRGGKGDLCIVLNVLLMQKLDPEHRALLKKIMPNPPKPKLAKRTSGFFSWLKNKFT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Tropheryma whipplei (strain Twist)
Length
348 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
38.52 kDa
Sequence
MEDLYGILGVDHNASVDEIRRAYRRLARELHPDINPDSADRFKAVTHAYNILSDPEQRQRYDRHVSGGFSSDFNLSDLFQSFFDTSAEFQRGSDLLVNIDIDLKTAIYGGSQVVKIDSLVVCDVCNGTRSEPGYKAEVCFDCNGSGVVRGEVRTTLGNLITQNTCSKCRGNGERIDHPCRRCYGNGSRSAPRDITINIPPGVETGMRIKIPNMGNAGGAMPGDLYVDCKVKEHPYFLRDGQDLYCRLDISLVDALLGTKVKIDSLDGELAVVIPALSQNRDVIRIANKGAVTLRGGKGDLCIVLNVLLMQKLDPEHRALLKKIMPNPPKPKLAKRTSGFFSWLKNKFT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Tropheryma whipplei (strain TW08/27)
Length
348 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
38.521 kDa
Sequence
MEDLYGILGVDHDASVDEIRRAYRRLARELHPDINPDSADRFKAVTHAYNILSDPEQRQRYDRHVSGGFSSDFNLSDLFQSFFDTSAEFQRGSDLLVNIDIDLKTAIYGGSQVVKIDSLVVCDVCNGTRSEPGYKAEVCFDCNGSGVVRGEVRTTLGNLITQNTCSKCRGNGERIDHPCRRCYGNGSRSAPRDITINIPPGVETGMRIKIPNMGNAGGAMPGDLYVDCKVKEHPYFLRDGQDLYCRLDISLVDALLGTKVKIDSLDGELAVVIPALSQNRDVIRIANKGAVTLRGGKGDLCIVLNVLLMQKLDPEHRALLKKIMPNPPKPKLAKRTSGFFSWLKNKFT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Tropheryma whipplei (strain Twist)
Length
348 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Similarity
Belongs to the DnaJ family.
Mass
38.52 kDa
Sequence
MEDLYGILGVDHNASVDEIRRAYRRLARELHPDINPDSADRFKAVTHAYNILSDPEQRQRYDRHVSGGFSSDFNLSDLFQSFFDTSAEFQRGSDLLVNIDIDLKTAIYGGSQVVKIDSLVVCDVCNGTRSEPGYKAEVCFDCNGSGVVRGEVRTTLGNLITQNTCSKCRGNGERIDHPCRRCYGNGSRSAPRDITINIPPGVETGMRIKIPNMGNAGGAMPGDLYVDCKVKEHPYFLRDGQDLYCRLDISLVDALLGTKVKIDSLDGELAVVIPALSQNRDVIRIANKGAVTLRGGKGDLCIVLNVLLMQKLDPEHRALLKKIMPNPPKPKLAKRTSGFFSWLKNKFT

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP)
Length
310 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity).
Similarity
Belongs to the DnaJ family.
Mass
32.918 kDa
Sequence
MAYKDYYEVLGVSRSASDSDIKSAYRKLAKQYHPDKNAGDESAAEKFKEIGEAYAVLSDPQKRQAYDQFGHTGQVPPGGYPGGGFQGGDFGGFDPSQFSDFFQEMFGGRAAGMGGRGGFTSPDGRPIDLEDLFGGLGGMGGAAQGGGRRFVQNVEGELQVSLSEAFEGSDEIINVDGRRLSLRVPAGTRDGARLRLAGQGPGGGDVLLTIRVLEDARFELDGDDLTTSVDVPAPVAALGGAVTVQTITGSGQLNVPAGSSGGRRMRLKGQGWPKKSGGRGDLYVRLNVTVPKELSEEERQLYEQLRDLQR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP)
Length
310 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity).
Similarity
Belongs to the DnaJ family.
Mass
32.918 kDa
Sequence
MAYKDYYEVLGVSRSASDSDIKSAYRKLAKQYHPDKNAGDESAAEKFKEIGEAYAVLSDPQKRQAYDQFGHTGQVPPGGYPGGGFQGGDFGGFDPSQFSDFFQEMFGGRAAGMGGRGGFTSPDGRPIDLEDLFGGLGGMGGAAQGGGRRFVQNVEGELQVSLSEAFEGSDEIINVDGRRLSLRVPAGTRDGARLRLAGQGPGGGDVLLTIRVLEDARFELDGDDLTTSVDVPAPVAALGGAVTVQTITGSGQLNVPAGSSGGRRMRLKGQGWPKKSGGRGDLYVRLNVTVPKELSEEERQLYEQLRDLQR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Synechococcus elongatus (strain PCC 7942)
Length
287 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity).
Similarity
Belongs to the DnaJ family.
Mass
31.98 kDa
Sequence
MQNFRDYYALLGIPQSADQAAIKAAFRKLARQCHPDLNPGDRQAEERFKQISEAYEILSDPDRRAEYQRFSRYWQQQGAASVGSDDDYGDFPDFDIFVDELLGRRTVERSPRRSARRSAATSSALSRDLERSLEVDPKTALQGGSAQLQLEDGRLLEVDIPAGIQAGEYLRLRGQGIKGGDLLLRVQLQASNFQVQGSDVIYTLNVSPAMAVLGGQVTVPTLDGPVQMKLPASLRSGQRLRLAGKGYSKPSGDRGDQIVVIQLQLPTRLSPEERQLYEQLRSLEQSR

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Onion yellows phytoplasma (strain OY-M)
Length
257 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity).
Similarity
Belongs to the DnaJ family.
Mass
28.229 kDa
Sequence
MTKKDYYHILGLDKDASPEDIKKAYRSLAKKYHPDISKEANAENKFKEVQEAYSVLGDASKKSNYDRFGDASDNGFSGFGGGGFDGFDSFGDSFFSSFGDIFGNQQTKKPSYDKKVEMTISFMDAVLGANKTIEITVEADCRVCHGKGAVSNQDVITCKRCGGNGQIITEQRTFLGNIRSRQVCPNCSGKGQEIKNKCYACHGQKRQKVKQSATFNIPAGIQEGMSLQVPGKGNFVPLSNNQKRRRSILLTFNSASS

Gene
dnaJ
Protein
Chaperone protein DnaJ
Organism
Streptococcus agalactiae
Length
24 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity).
Similarity
Belongs to the DnaJ family.
Mass
2.76 kDa
Fragment
single
Sequence
MNNTEFYDRLGVSKDASQDEIKKA