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dnaJ2

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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
41.416 kDa
Sequence
MNNAEWANKDYYADLGVSKNASAEDIKKAYRKLARENHPDKNPGDKVAEDRFKKAAEAYDVVGDETKRREYDDLKKLLASGGIRGGFGSGGADFPGGFRSTQGFDASDLFGGAGPGGGFSADGGLGDIFGGIFNRGSSPRQSARPTRGADVETDITLEFREAAKGTTIPVELTGEAPCNTCHGSGSASGQPSKCGQCNGSGFTSENKGAFGFSAPCTNCGGTGEVITDPCVDCRGRGTVRRTRSITVRIPAGVEDGQKVRLAGQGEAGPNGKPAGDLFVRVHVKEDPVFEREGNNIHVTVPVSFSELALGGAISVPTLDKPVKLKLAPGTPDGRTLRVRGRGVETRTAKGDLMVTVQVTVPPTLSDEAAEALRTYAEAEKKSGFDPRANWAGNNR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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
41.036 kDa
Sequence
MNNSEWANKNYYADLGVSSSASEDEIKKAYRKLARENHPDKNPGDKAAEDRFKKAAEAYDVLGDDKKRKEYDELKALLASGGIRGGFGSGGAGFPGGFRTSTGGFDTSDLFGGGQGGGFSTDGGLGDIFGGLFNRGAGSHQSARPTRGADVQTEITLSFVEAAKGTTIPVELTGDAPCNTCHGSGSKSGHPAKCGTCDGTGFTSENKGAFGFSAPCATCGGTGEIITDPCDNCHGRGTVRKSRSITVRIPTGVEDGQKVRLAGQGEAGPNGKPAGDLFVKVHVKKDDVFTRDGSNILITIPVSFSELALGGAISVPTLNKPVKLKLPAGTPDGRTLRVRGRGIEARDSTGDLLVTVQVSVPKNLDDNAAEALRAYAEAETNSGFDPRANWAGQNR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
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
41.28 kDa
Sequence
MAQREWVEKDFYKELGVSSDASPEEIKRAYRKLARDLHPDANPDNPAAGERFKAVSEAHNVLSDPAKRKEYDETRRLFAGGGFGGRRFDTGGFGGFNVGGDGAEFNLNDLFDAAGRSGGTNIGDLFGGLFGRASGGRPSRPRRGNDLETETQLDFVEAAKGVAMPLRLTSPAPCTNCHGSGARPGTSPKVCPTCNGSGVISRNQGAFGFSEPCTDCRGSGSIIEHPCDECKGTGVTTRTRTINVRIPPGVEDGQRIRLPGQGEAGLRGAPSGDLYVTVHVRPHKVFGRDGDDLTVTVPVSFTELALGSTISVPTLDGKVGVRVPKGTADGRILRVRGRGVPKRSGGHGDLLVTVKVAVPPNLDGAAQEALEAYAAAERASGFDPRAGWAGNR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
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
40.713 kDa
Sequence
MAAKNEWAEKDYYADLGVSSSATEAEIKKAYRKLARENHPDSHPGDAAAEERFKKVAEAYDVVGDETKRKEYDEFRSMIASGGFGGAGFPGGFRTQEGFDFDLGDIFGSGAGRGHAPQGGFGDIFGGIFNRGGGARNAARPTRGSDVETEITLEFREAAKGTTIPLQLTGDAPCHTCHGSGSRSGAPTTCTECNGTGFTSENKGAFGFSAPCTQCGGTGKMISDPCPDCSGTGTQRRTRSITVRIPAGVVDGQKVRLAGQGEAGPNGLPAGDLYVTVHVKNDRVFTRSGDDLEVTVPVSYAELALGDTISVPTLDLPVRVRIPSGTPNGRVLRVRGKGVPKRGGSAGDLLVKVEVTVPSSLDAASASALRAYVQAERDAGFDPRAGWAGK

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Nocardia farcinica (strain IFM 10152)
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
40.274 kDa
Sequence
MSQREWIEKDYYKELGVSSTASQDEIKKAYRKLARDLHPDANPGDSKAEERFKAVSEAHAVLSDPAKRKEYDETRRLFAGGGYPRGGFGPGGAGGFSQGFDIGDIFGGTAAGDGGLGDILGGLFNRGGTRTTSRPRRGADVETETTLGFREAAQGVTVPLRMTSPSPCTTCHGSGAKPGTSPRVCPICNGTGVVSRNQGAFGFSEPCDGCRGTGSIIDDPCVDCHGSGIQNRTRTITVRIPPGVSDGQRIRLAGQGEAGLRGAPSGDLYVTVHVSQDKVFGRNGDDLTLVLPVSYAELVLGTTVSVPTLDGRVGVKVPPGTADGRTLRVRGRGVPKRGGGAGDLLVTVKVAVPQKLDDDALEALERYREAEKASGFDPRAGWAGA

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
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
40.489 kDa
Sequence
MARDYYGLLGVSKNASDADIKRAYRKLARELHPDVNPDEAAQAKFKEISVAYEVLSDPDKRRIVDLGGDPLESAAAGGNGFGGFGGLGDVFEAFFGGGFGGGAASRGPIGRVRPGSDSLLRMRLDLEECATGVTKQVTVDTAVLCDRCQGKGTNGDSVPIPCDTCGGRGEVQTVQRSLLGQMLTSRPCPTCRGVGVVIPDPCQQCMGDGRIRARREISVKIPAGVGDGMRVRLAAQGEVGPGGGPAGDLYVEVHEQAHDVFVREGDHLHCTVSVPMVDAALGVTVTVDAILDGLSEITIPPGTQPGSVITLRGRGMPHLRSNTRGDLHVHVEVVVPTRLDHQDIELLRELKGRRDREVAEVRSTHAAAGGLFSRLRETFTGR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
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
40.489 kDa
Sequence
MARDYYGLLGVSKNASDADIKRAYRKLARELHPDVNPDEAAQAKFKEISVAYEVLSDPDKRRIVDLGGDPLESAAAGGNGFGGFGGLGDVFEAFFGGGFGGGAASRGPIGRVRPGSDSLLRMRLDLEECATGVTKQVTVDTAVLCDRCQGKGTNGDSVPIPCDTCGGRGEVQTVQRSLLGQMLTSRPCPTCRGVGVVIPDPCQQCMGDGRIRARREISVKIPAGVGDGMRVRLAAQGEVGPGGGPAGDLYVEVHEQAHDVFVREGDHLHCTVSVPMVDAALGVTVTVDAILDGLSEITIPPGTQPGSVITLRGRGMPHLRSNTRGDLHVHVEVVVPTRLDHQDIELLRELKGRRDREVAEVRSTHAAAGGLFSRLRETFTGR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 (By similarity). Inhibits the beta-lactamase and RNase activity of RNase J.
Similarity
Belongs to the DnaJ family.
Mass
40.489 kDa
Sequence
MARDYYGLLGVSKNASDADIKRAYRKLARELHPDVNPDEAAQAKFKEISVAYEVLSDPDKRRIVDLGGDPLESAAAGGNGFGGFGGLGDVFEAFFGGGFGGGAASRGPIGRVRPGSDSLLRMRLDLEECATGVTKQVTVDTAVLCDRCQGKGTNGDSVPIPCDTCGGRGEVQTVQRSLLGQMLTSRPCPTCRGVGVVIPDPCQQCMGDGRIRARREISVKIPAGVGDGMRVRLAAQGEVGPGGGPAGDLYVEVHEQAHDVFVREGDHLHCTVSVPMVDAALGVTVTVDAILDGLSEITIPPGTQPGSVITLRGRGMPHLRSNTRGDLHVHVEVVVPTRLDHQDIELLRELKGRRDREVAEVRSTHAAAGGLFSRLRETFTGR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Cutibacterium acnes (strain DSM 16379 / KPA171202)
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
40.572 kDa
Sequence
MSTKDWAEKDYYKILGVSKDAKPEEIKKAFRKIARDNHPDSHPGDKAAEARFKEASEANDVLSNAKKRKEYDQARSLFGSAGGFRFPRGGAQTSVNVEDFLRTASNGDGFGDLFGNLFGASGGRRTASRSPRRGADVEGETTISFDDAVSGTTVTMDMVSQAPCQACRGTGARAGTVPRVCSTCQGSGMHASSAGGVFEMTEPCPDCHGRGMIVEDPCQVCHGSGRAKSTKSMQTRIPAGVEDGQRIRIKGKGSPGENGGKAGDLYVKVTVRPHEIFGRDGHNLTVTVPVTFPEATLGAEVEVPTLAGTTVRLRIPAGTPNGRTFRVRGRGVPRSDGSRGDLLATVEIAVPESLDDDARHVVERLRDSLPQATPRPWEVK

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Streptomyces albus G
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
40.668 kDa
Sequence
MATDYYAVLGVRRDASQDEIKKAFRRLARELHPDVNPDPKTQERFKEINAAYEVLSDPQKKQVYDLGGDPLSQNGGGGAGGFGQGGFGNFSDIMDAFFGTASQRGPRSRTRRGQDAMIRLDIELDEAAFGTTKDIQVDTAVVCNTCNGEGAAPGTSAQTCDMCRGRGEVSQVTRSFLGQVMTSRPCPQCQGFATVVPTPCPECAGDGRVPSRRTLTVKIPAGVDNGTRIQLAGEGEVGPGGGPGGDLYVEIHELPHSVFQRRGDDLHCTVTIPMTGPRPSAPRCLETLDGMEEIDIRPGTQSGQSVPLHGRGITHLRGGGGRDLIVHVEVTTPGKLDAEQEHLLRELAKLRGEERPTGQFQPGQQGLFSRLKDAFNGRS

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Mycobacterium leprae (strain TN)
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
40.4 kDa
Sequence
MARDYYGLLGVSRNASDADIKRAYRKLARELHPDINPDEAAQAKFKEISMAYEVLSDPEKRRIVDLGGDPMENAAASPSGFGGFGGLGDVFEAFFGGSSASRGPIGRVRPGSDSLLPMWLDLEECATGVTKQVTVDTAVLCDRCQGKGTNGDSAPIPCDTCGGRGEVQTVQRSLLGQMVTARPCPTCRGVGVVIPDPCCQCVGDGRVRARREITVKIPSGVGDGMRVRLAAQGEVGPGGGPAGDLYVEVHEQAHDIFVRDGDDLHCTVSVPMVDAALGTTITVDAILDGMSEIDISPGTQPGSVIELRGQGMPHLRSNTRGNLHVHVEVMVPTRLDQHDTELLRELKRRRSRDVAEVRSTHAAGGGLFSRLRETFTNR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
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
40.567 kDa
Sequence
MATDYYAVLGVRRDASQDEIKKAFRRLARELHPDVNPDPKTQERFKEINAAYEVLSDPQKKQVYDLGGDPLSQSGGGGAGGFGAGGFGNFSDIMDAFFGTASQRGPRSRTRRGQDAMIRVEIELDEAAFGTTKDIQVETAVVCTTCSGEGAAPGTSAQTCDMCRGRGEVSQVTRSFLGQVMTSRPCPQCQGFGTVVPTPCPECAGDGRVRSRRTLTVKIPAGVDNGTRIQLAGEGEVGPGGGPAGDLYVEIHELPHQTFQRRGDDLHCTVTIPMTAAALGTKVPLETLDGMEEVDIRPGTQSGQSIPLHGRGITHLRGGGRGDLIVHVEVTTPTKMDPEQERLLRELAKLRGEERPTGQFQPGQQGLFSRLKDAFNGR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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
40.488 kDa
Sequence
MATDYYAVLGVRRDASQDEIKKAFRRLARELHPDVNPDPKTQERFKEINAAYEVLSDPQKKQVYDLGGDPLSQAAGGGAGGFGAGGFGNFSDIMDAFFGTASQRGPRSRTRRGQDAMIRIEVELDEAAFGTTKDIQVDTAVVCNTCNGEGAAPGTSAQTCDMCRGRGEVSQVTRSFLGQVMTSRPCPQCQGFGTVVPTPCPECAGDGRVRSRRTLTVKIPAGVDNGTRIQLAGEGEVGPGGGPAGDLYVEIHELPHSTFQRRGDDLHCTVTIPMTAAALGTKVPLETLDGMEEVDIRPGTQSGQSIPKHGRGVTHLRGGGRGDLIVHVEVTTPGKLDPEQERLLRELAKLRGEERPTGQFQPGQQGLFSRLKDAFNGR

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Aquifex aeolicus (strain VF5)
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
41.963 kDa
Sequence
MASSTKKDYYEILGVPRNASQEEIKKAYRRLVRKYHPDICKKPECEEKFKEINEAYQVLSDPEKRKLYDMYGHAAFEGAGAQQRVETTEIPPIEEILREFFDFDIGSIFERATGRRRARRRRSVKGEDIVVPVEITLEEAFKGTTVPIEVEREVPCSACGGTGYDESKSRTCPTCGGRGETVQGNWFFQVRQTCPTCGGEGVIYENCHACTGRGYGLVKETIKVKIPPGVRDGSKLVVEGKGHAGRYGGPPGDLYIIVKVKPHKIFERKGDDLYVDVNITYPEAVLGTEVEVPTLDGEKVKVKIPPGTKEGELIKVPGKGMPRLKGSGRGDLYVRVHIDVPKIGVLSKLLGDGKKVEELLKQLQEVLPKPERIVER

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Aromatoleum aromaticum (strain EbN1)
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
40.982 kDa
Sequence
MAKRDYYEVLGVNRDASDNEIKKAYRKLAMKHHPDRNPDNKDSEDHFKEAKNAYEILSDAQKRAAYDRYGHAGVDPSAGAGPGGQGFDGFADAFSDIFGDIFGGAGGAGRGRSNVYRGADLRYNLEISLEEAARGADKTIRIPTVEECETCHGSGAKPGTQPKPCPTCGGAGQVRIQQGFFSIQQTCPKCHGTGRIIPDPCRDCGGAGRVKRQKTLEVKIPAGIDEGMRLRHAGHGEPGVNGGPPGDLYVEIHIRAHPVFQRDHDDLHCEMPISITTAALGGEIEIPTLEGMARLKIPAETQSGKVFRLRGKGIRNVRSQAHGDLMCHVVVETPVNLTERQKELLREFEEVSSSDADRHNPKAKSWMDKVKDFFGA

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
307 amino acids
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE 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
34.698 kDa
Sequence
MEQVRNYYQILGVPRNATAEEIKKSFRKLARQYHPDVNPNDKTAEEKFKDINEAYDVLSDETKRRELDSRLFGRFRRPPTSRFSPNSNGGRSPNGTSVNGQVRTPTGRTGTRQPAQSWQDFSETRRTKVVSPARPVPRDVEANLTLPLEKAYRGGKERIRLEDGRSLEVEMPGGMGDGQRIRLKQQGINGGDLYLKINLSPHPLFTLQGTDIACQVPVTPSEAILGGAIEVMTIDGLVKMTVPAGLKNGQKLRLAKKGFPNNQGDRGDQLVEIRVEIPPEPSPEELELYRRIREKETFNPRQKFFDF

Gene
dnaJ2
Protein
Chaperone protein DnaJ 2
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Length
280 amino acids
Function
Does not influence ATP binding or hydrolysis nor ADP release. Exerts influence on the interaction of DnaK with substrates; in the presence of DafA, DnaJ inhibits substrate binding, and substrate already bound to DnaK is displaced by DnaJ and DafA.
Similarity
Belongs to the DnaJ family.
Mass
30.978 kDa
Sequence
MAAKKDYYAILGVPRNATQEEIKRAYKRLARQYHPDVNKSPEAEEKFKEINEAYAVLSDPEKRRIYDTYGTTEAPPPPPPGGYDFSGFDVEDFSEFFQELFGPGLFGGFGRRSRKGRDLRAELPLTLEEAFHGGERVVEVAGRRVSVRIPPGVREGSVIRVPGMGGQGNPPGDLLLVVRLLPHPVFRLEGQDLYATLDVPAPIAVVGGKVRAMTLEGPVEVAVPPRTQAGRKLRLKGKGFPGPAGRGDLYLEVRITIPERLTPEEEALWKKLAEAYYARA