grpE

Protein GrpE

298 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

33.406 kDa

MANENIQIKSSLDDLKNFVQNPKSQNQKIKAVNQLMYNEFVKIETAINNINNYIENLTHRLELTNENFKTKVQEVESKAQQKINDRIEELDKRKKEEIENAKKYAIEKSIDSAINIVDQLEIALEFASLDPAVKNYVSGFKMVLNSFVNWLASVNIHRMDIKPGDKFDEKYMSASDKASDPDYPADHVCKVMKSGYKLYDRVVRHAMVAVSDGVGYVEPASSEQEQPQTPAKSTQTPPAQETASAPAKTKPTAPPTNNLNANKPPVVSNPPHQKPVQPPQSNTPGPKQPITHQVIKKS

grpE

Protein GrpE

286 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

32.276 kDa

MSEDNRPLEEQLGNRAESPNTPESVREDNSKSQNNHLNQPSSTPQTPETTADNTFVESELLQDSQGIEKLLATLAEQIGSTQEGQEILGQLQPLLTNLIQQNESLLQTNQSLKDQLEEQNQQIDAAKRRYIGLAAEFDNFRKRTLREKEELEKQAKRKTLSELLTVVDNFERARLQIKPSNEGEGEIHKSYQGVYKNLVDSLKRLGVSAMRAEGEPFDPMYHEAMLREPTNDFPEGTVIEQLVRGYLLDDQVLRHAMVKVAAPKEPDSSETESTSESVSDVQQPTT

grpE

Protein GrpE

264 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

30.542 kDa

MQEFMNFEECSKQNTNNCKQHEKNIDENNCSCKEKKVQSKKVSSDHSSSEDNASSDINSNKAETLTLNCGDQSDNKNSISDIESNKFIPNENDFQMLKKQLNDLKAENVNLKRDLQEAHQQRTNDNLKYLADFDNFKKRITVQTNREIKYALTDFIKNILIPLEQFEKVLEMPKVDDSVKSFLLGFKMIHKQVKDILQKEGVEEIKALGVKFDPNFHYALEKISDLKQPNGINVLVLQKGFLYKDLVIKPAMVKVNEWSDKNND

grpE

Protein GrpE

259 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

29.009 kDa

MNSDVSSSEHELSQDGSSQNNPSENFVSSSNSNESVNQVELSDNPEVEHQVKNDSVDTAKEQSSTSCESNIKGSDTEARLQQLEKEHETLNSQYMRIAADFDNFRKRQTRDQDDLKIQLTCTTLSEILPIVDNFERARQQLNPEGEEAQALHRSYQGLYKQLVEVLKNLGVAPMRVVDQAFDPSLHEAVMREPSDEKAEDIVIEELQRGYHLNGRVLRHALVKVSMGPGPKAVNEEIPDQSASNQELSESVDGPTKDEN

grpE

Protein GrpE

259 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

28.936 kDa

MNSDVSSSEHELSQDGSSQNNPSENSVSSPNSNESVNQVELSDNPEVEPQVKNDSVDTANEQSSTSCESNIKGSDTEARLQQLEKEHETLNSQYMRIAADFDNFRKRQTRDQDDLKIQLTCTTLSEILPIVDNFERARQQLNPEGEEAQALHRSYQGLYKQLVEVLKNLGVAPMRVVDQAFDPSLHEAVMREPSDEKAEDIVIEELQRGYHLNGRVLRHALVKVSMGPGPKVINEEIPDQSASNQELSESVDGSTKDEN

grpE

Protein GrpE

259 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

29.009 kDa

MNSDVSSSEHELSQDGSSQNNPSENFVSSSNSNESVNQVELSDNPEVEHQVKNDSVDTAKEQSSTSCESNIKGSDTEARLQQLEKEHETLNSQYMRIAADFDNFRKRQTRDQDDLKIQLTCTTLSEILPIVDNFERARQQLNPEGEEAQALHRSYQGLYKQLVEVLKNLGVAPMRVVDQAFDPSLHEAVMREPSDEKAEDIVIEELQRGYHLNGRVLRHALVKVSMGPGPKAVNEEIPDQSASNQELSESVDGPTKDEN

grpE

Protein GrpE

259 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

28.936 kDa

MNSDVSSSEHELSQDGSSQNNPSENSVSSPNSNESVNQVELSDNPEVEPQVKNDSVDTANEQSSTSCESNIKGSDTEARLQQLEKEHETLNSQYMRIAADFDNFRKRQTRDQDDLKIQLTCTTLSEILPIVDNFERARQQLNPEGEEAQALHRSYQGLYKQLVEVLKNLGVAPMRVVDQAFDPSLHEAVMREPSDEKAEDIVIEELQRGYHLNGRVLRHALVKVSMGPGPKVINEEIPDQSASNQELSESVDGSTKDEN

grpE

Protein GrpE

255 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.411 kDa

MTVIEVEASGPSTPVEAEASASPADTTSPPSDAEATPSEDVAALRQEVESLKAQLEFSQAKGRETMERLREAHERAKEAQERTVRHAADLENYRKRAQKEKEEVQRFGSEKLLKDLLPVMDNLDRAIDAAAKSPDLDSFEKGVAMTRKSFEDALGRHGVKGFSAKGQVFDPRVHEAIQQVETADVPAGHVAYEVVRGFYLNERLVRPAMVVVARAPAEPVAAAEPPAVAEPATATTDTEAPAAPAQSENSSGGSQ

grpE

Protein GrpE

252 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.766 kDa

MHNPQSRGHNLSQAMSDQTVTNPAAEAQEGEITPDTPDTVDKVENTPVENVENPAEATPGEEDQASEATSANAADLLEQIAALEAAKASLSQVVEERNSQYIRLAADFENFRKRTQREKEELELQIKCSVIADLLPVVDSFELARTHIQTETEAEEKIHRSYQGVYKQLVECLKRIGVSAMQAKGKPFDPNLHEAVLREATNEHPEGTVIEELKRGYMLGDRVLRHAMVKVAAPPEEGSASNTNPTNDVTDV

grpE

Protein GrpE

249 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.568 kDa

MNEDQVSLENQTNPVSPEASDVPAVTPEESPQPTDAVLGEPSGEQSEDPRIGAATETEGGPLEQEKSSEEIIAILQKDLASHRQELAEQSEQLDSIKKRYVALAAEFDNFRKRTQREKEEQAKLIKGRTITELLPVVDNFERARTQIKPNSDGENQIHKSYQGVYKNLVDSLKGLGVAPMRPEGKPFDPKYHEAMLREPTAEYPEDTVIEELVRGYLLDDIVLRHSMVKVAVAPEEGAEVVNGEAGANP

grpE

Protein GrpE

248 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.934 kDa

MIDENKQVNHTSQQLGESTEVKQAIMSESPAQINNNESANEVTEPVAIPTNVVGDTTATEDNGFTATQIQEANTAALAELTQQISSLKTQLDERSTQYMRIAADFENYRKRTQKEKEELDLQVKRNTILELLPIVDNFERARSHLKPQTESEMTIHKSYQGVYKQLVDSLKRLGVSPMRPEGQEFDPNLHEAVMREPTDEHPEGTVLEELVRGYYLGDRVLRHSMVKVAAPKEDTLPAQENQSSPADS

grpE

Protein GrpE

248 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.981 kDa

MIDENKQVNHTSQQLGESTEVKQAIMSESPAQINNNESTNEVTESVAIPTNVVGDTTATEDNGFTATQIQEANTAALAELTQQINSLKTQLDERSTQYMRIAADFENYRKRTQKEKEELDLQVKRNTILELLPIVDNFERARSHLKPQTESEMTIHKSYQGVYKQLVDSLKRLGVSPMRPEGQEFDPNLHEAVMREPTDEHPEGTVLEELVRGYYLGDRVLRHSMVKVAAPKEDTLPAQENQSSPADS

grpE

Protein GrpE

247 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

28.973 kDa

MFLEKDQDNLDNLETQAKELHKDCKECKNCQKEETKTTNKDNQKEDETVKNQSNQSNQSNQTKQTNTKQQKHQPKENSHLQITKLQTQIKELQQQLTQQKKSFDEELLKNQAELINFKKRAQTQKANELKYASSNFITNLLMPLEQLEKVIDMPTQNELLQKYLLGFKLLQQQIKKVLQDEGVEEIEALNKPFDPALHHALETVCDPKKPDKTNLAVLQKGYLYKKRILRPTLVKVNEWSDKNDKNE

grpE

Protein GrpE

247 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.48 kDa

MNDEASTPIQEDLKEESAVDLAQEAKPTSDEPSLSNVAEGSQEAGAETDVTSSDAKDSSSQALDNEARLEQLEREHETLNSQYMRIAADFDNFRKRQSRDQDDLRLQLQCNTLSSILPVVDNFDRARQQLNPEGEEAQALHKSYQGLYKQLVDVLKQLGVAPMRVVGQTFDPSLHEAVLREPSDELAEDIIVEELQRGYHLNGRVLRHALVKVSMGPGPKDDGEETITEQSLEGDNTTDQQSSEKSD

grpE

Protein GrpE

247 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.948 kDa

MKKNHEKHADKKEAAKEELEKDLQPKDESAVKDEQGAGCGCETSKENPQEDKAEQNSSTGGKCEKNDDVLSPEKRIEELEAKCRDWQDQYLRKAADFENYRKRMIREKQEAIDYANSNLLLDLVQVLDDFDRAIDAGKTQGGESVNNAFVEGVVMIKNQMVSMLSSKYGLSYYPAKGEAFDPNLHEAVSMIQSPDVKEAVVGEELQKGYKLKERVIRHSKVMVLMPAEKQDEKKAEESEAADKKNEN

grpE

Protein GrpE

247 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.48 kDa

MNDEASTPIQEDLKEESAVDLAQEAKPTSDEPSLSNVAEGSQEAGAETDVTSSDAKDSSSQALDNEARLEQLEREHETLNSQYMRIAADFDNFRKRQSRDQDDLRLQLQCNTLSSILPVVDNFDRARQQLNPEGEEAQALHKSYQGLYKQLVDVLKQLGVAPMRVVGQTFDPSLHEAVLREPSDELAEDIIVEELQRGYHLNGRVLRHALVKVSMGPGPKDDGEETITEQSLEGDNTTDQQSSEKSD

grpE

Protein GrpE

247 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.948 kDa

MKKNHEKHADKKEAAKEELEKDLQPKDESAVKDEQGAGCGCETSKENPQEDKAEQNSSTGGKCEKNDDVLSPEKRIEELEAKCRDWQDQYLRKAADFENYRKRMIREKQEAIDYANSNLLLDLVQVLDDFDRAIDAGKTQGGESVNNAFVEGVVMIKNQMVSMLSSKYGLSYYPAKGEAFDPNLHEAVSMIQSPDVKEAVVGEELQKGYKLKERVIRHSKVMVLMPAEKQDEKKAEESEAADKKNEN

grpE

Protein GrpE

243 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

28.326 kDa

MIINYKFSDFYFDKKLSGKEVEFSIQIQKREASSDKNLQSKNLIIDAINVQRDFSEKNKSSDNLEILNKQIEDKNDLIINLEKKVFDLTLENKKNIDDFNEKAKSFAKKAQEELDKYKLELKSFLENEFEEKKKFSFQKLFENIINPLNNFRLAIDAGSKQENSSIKSYVQGFEMLLNQTINILESYGLIIIRPEIGDTFNPEVHNAVELREEGTPNRILKINSLGYQFHERVLKPASVIVSK

grpE

Protein GrpE

242 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.676 kDa

MKEEVSTSNQEDLVADQEVIASEESDLSPKEEKVSESTIDDDDSLNDAELQSNKQTLDNEARLEQLEKEHETLRSQYVRIAADFDNFRKRQSRDQDDLKLQLTCNTLSEILPVVDNFERARQQINPEGEEALTIHRNYQNLYKQLVDVLKKLGVAPMRVVGQSFDPTLHEALLREPSELMVEDMILEELVRGYHLNGRVLRHAQVKVSMGPGPKVDEEDKQIDEDSQADKRDEATTASNELD

grpE

Protein GrpE

242 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.554 kDa

MAGENSSTETKNQEINEKTPEVQTFETNVEFESSQKVESDTELSADNASIDTDIQSTESTSKEKDQVLLKEAYELLQTQLETTKYQLEEKESQYKRLGADFDNFRKRTQKEKEDLDTQVKCSTIMELLPVIDNFERARSHIKPANDGEMAIHKSYQSVYKQMVDSLKRLGVSVMRPEGQEFDPNLHEAVMREATAEHPEGTVIEELVRGYILGERVLRHAMVKVATAPDTDAETENQTDPES

grpE

Protein GrpE

242 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.676 kDa

MKEEVSTSNQEDLVADQEVIASEESDLSPKEEKVSESTIDDDDSLNDAELQSNKQTLDNEARLEQLEKEHETLRSQYVRIAADFDNFRKRQSRDQDDLKLQLTCNTLSEILPVVDNFERARQQINPEGEEALTIHRNYQNLYKQLVDVLKKLGVAPMRVVGQSFDPTLHEALLREPSELMVEDMILEELVRGYHLNGRVLRHAQVKVSMGPGPKVDEEDKQIDEDSQADKRDEATTASNELD

grpE

Protein GrpE

242 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.554 kDa

MAGENSSTETKNQEINEKTPEVQTFETNVEFESSQKVESDTELSADNASIDTDIQSTESTSKEKDQVLLKEAYELLQTQLETTKYQLEEKESQYKRLGADFDNFRKRTQKEKEDLDTQVKCSTIMELLPVIDNFERARSHIKPANDGEMAIHKSYQSVYKQMVDSLKRLGVSVMRPEGQEFDPNLHEAVMREATAEHPEGTVIEELVRGYILGERVLRHAMVKVATAPDTDAETENQTDPES

grpE

Protein GrpE

242 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.673 kDa

MSDDFAESVTEANAESDTETAADAESSAAEDASAADDAAPEESTGDEQAGETTAESSDAESVTVSERVAEYDDELAAEVEALEARVADLEASVADLETERDEAEETASDLESRLKRTQADFQNYKKRAKKRQQQIKERATEDFVERVVTVRDNLVRALDQDEDADIRDGIESTLKEFDRILEDENVEIIDPEPGTDVDPTRHEVMMRVESDQPADTIADVFQPGYEMAEKVIRAAQVTVSKE

grpE

Protein GrpE

241 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

28.573 kDa

MFLEKEQDNLDNLKTQTKELHKDYTECQNCQKEETQTTNKDNQKEDETFKNQPNKTKQTNTKQQKHLSKESSHQQITKLQTQIKELQQKLSQQKKTFDEGLLKNQAEFINFKKRAQTQKENELKYASSNFINNLLMPLEQLEKVIDMPTQNELLQKYLLGFKLLQKQIKKVLQDEGVEEIEALNKPFDPTFHHALETVCDFEKPDKTNLAVLQKGYLYKKRILRPTLVKVNEWSDKNEKNE

grpE

Protein GrpE

240 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.16 kDa

MTDNQRQSTTDGQPETRDPAQATAEAAEQTQATQASAAVEGELQDGSADSATGASLSADDGADPEALRQRVEELEKALADAEQKAEEHWDQVLRMRAELENARRRAEKDVDQAKRQGLEKVCGDLLQVKDSLEMGVQAAEDAEADREKLLEGSQLTLKMLNQVFERFEIEEINPQGERFNPDYHEAMAAQPSDEQEPNTVLQVVQKGYRLQDRLLRPALVVVAKKGDGGAGSGGSVDETA

grpE

Protein GrpE

240 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.12 kDa

MSGDASTPEQDPAQVVADGQQPVETPNDPVETPSASDPGSAAEVSPQTGNNEARLEQLEREHTTLRDEHDVLRGQYMRIAADFDNFRKRQSRDQDDLKIQLTCSTLSEILPVVDNFERARQQLDPQGEEAQALHRSYQGLYKQLVDVLKQLGVAPMRVVGQEFDPTLHEAVLREPSDAHPEDVVIEELQRGYHLNGKVLRHAMVKVSMGPGPQDGASSQPAEAPAADAPAEDSGSGDGNG

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.443 kDa

MIENQSDNIDNKEIDVSIQDNAPEDKSSMQNSTTENDELSSQKTEEINTEELKNTISNNDARLEQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKIQLVSKTLTAILPIVDNFERARQQLKPESEEAQALHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPNLHEAVLREPSEEFEEDFIIEELQRGYHLEGKVLRHALAKVSMGPGKQKSQQEVEKDTVEGDVDSDANTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.49 kDa

MIENQSDNIDNKEKDVSNQDNAPEDISSEQNSTNENDELTSQKKEAINTEELKNTISNNDARLKQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKIQIVSKTLTAILPIVDNFERARQQLQPESEEAQALHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPNLHEAVLREPSEESDEDFIIEELQRGYHLEGKVLRHALVKVSMGPGKQNSQQEVEKDTVEEDVNSEVNTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.475 kDa

MIEEQSDNVENKDENVSMDNNISENLPIAEEQTNEDKKLPDDNNEKIDAEDLKNTITNNDARLEQLEKEHETLKSQYVRIAADFDNFRKRQSRDQDDLKIQLVSKALTAILPIVDNFERARQQLKPEGDEAQTLHRSYQGLYKQLVEVLKQQGVAPMRVVGQQFDPNLHEAVLREPSEEQNEDIIIEELQRGYHLEGKVLRHALVKVSMGPGQQISQESEEKDKVDKDIDSEGSISEEN

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.567 kDa

MIENQSDNIDIKENDVLNQDNAPEDNSSAAEKTIENDELSPQKTEEINTEELKNTISNNDARLEQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKVQLVSKTLTAILPIVDNFERARQQLKPESEEAQALHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPNLHEAVLREPSEEFKEDLIVEELQRGYHLEGKVLRHALVKVSMGHGQQNSQEEVEKDTVEEDIDSEENTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.671 kDa

MIEKQSDNVENLEDNVSQEVNKNEDSSVIENQTSEDKQTLEVDDENIYAEDLKNTITNNDARLEQLEKEHETLKSQYVRIAADFDNFRKRQSRDQDDLKVQLVSKALTAILPIVDNFERARQQLKPESEEAQTLHRSYQGLYKQLVEVLKQQGVSPMRVVAQQFDPKLHEAVLREPSQEFNEDIIIEELQRGYHLEGKVLRHALVKVSMGPGQQNSQEPEEKDKVEEDIDSENPISEEN

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.528 kDa

MIENQSDNIDNKENDLSDQDNALENVSSAQELTTENNELSSQKTEEINTEELKNSISNNDARLEQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKIQLVSKTLTAILPIVDNFERARQQLKPESEEAQSLHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPSLHEAVLREPSEKFEEDFIIEELQRGYHLEGKVLRHALVKVSMGPGKQNSQEEVEKDKVEGDIDSEENTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.443 kDa

MIENQSDNIDNKEIDVSIQDNAPEDKSSMQNSTTENDELSSQKTEEINTEELKNTISNNDARLEQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKIQLVSKTLTAILPIVDNFERARQQLKPESEEAQALHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPNLHEAVLREPSEEFEEDFIIEELQRGYHLEGKVLRHALAKVSMGPGKQKSQQEVEKDTVEGDVDSDANTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.49 kDa

MIENQSDNIDNKEKDVSNQDNAPEDISSEQNSTNENDELTSQKKEAINTEELKNTISNNDARLKQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKIQIVSKTLTAILPIVDNFERARQQLQPESEEAQALHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPNLHEAVLREPSEESDEDFIIEELQRGYHLEGKVLRHALVKVSMGPGKQNSQQEVEKDTVEEDVNSEVNTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.475 kDa

MIEEQSDNVENKDENVSMDNNISENLPIAEEQTNEDKKLPDDNNEKIDAEDLKNTITNNDARLEQLEKEHETLKSQYVRIAADFDNFRKRQSRDQDDLKIQLVSKALTAILPIVDNFERARQQLKPEGDEAQTLHRSYQGLYKQLVEVLKQQGVAPMRVVGQQFDPNLHEAVLREPSEEQNEDIIIEELQRGYHLEGKVLRHALVKVSMGPGQQISQESEEKDKVDKDIDSEGSISEEN

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.567 kDa

MIENQSDNIDIKENDVLNQDNAPEDNSSAAEKTIENDELSPQKTEEINTEELKNTISNNDARLEQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKVQLVSKTLTAILPIVDNFERARQQLKPESEEAQALHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPNLHEAVLREPSEEFKEDLIVEELQRGYHLEGKVLRHALVKVSMGHGQQNSQEEVEKDTVEEDIDSEENTSEDV

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.671 kDa

MIEKQSDNVENLEDNVSQEVNKNEDSSVIENQTSEDKQTLEVDDENIYAEDLKNTITNNDARLEQLEKEHETLKSQYVRIAADFDNFRKRQSRDQDDLKVQLVSKALTAILPIVDNFERARQQLKPESEEAQTLHRSYQGLYKQLVEVLKQQGVSPMRVVAQQFDPKLHEAVLREPSQEFNEDIIIEELQRGYHLEGKVLRHALVKVSMGPGQQNSQEPEEKDKVEEDIDSENPISEEN

grpE

Protein GrpE

239 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.528 kDa

MIENQSDNIDNKENDLSDQDNALENVSSAQELTTENNELSSQKTEEINTEELKNSISNNDARLEQLEKEHETLKNQYVRISADFDNFRKRQSRDQDDLKIQLVSKTLTAILPIVDNFERARQQLKPESEEAQSLHRSYQGLYKQLVEVLKQQGVSPMRVVGQQFDPSLHEAVLREPSEKFEEDFIIEELQRGYHLEGKVLRHALVKVSMGPGKQNSQEEVEKDKVEGDIDSEENTSEDV

grpe

GrpE protein homolog, mitochondrial

238 amino acids

Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mtHSP70 (hsp70-5) to substrate proteins (By similarity).

Belongs to the GrpE family.

26.827 kDa

MLRTALTRSSRALCSGARVAAQRPIASQIFQMQAARTAAPQLRSAARWYSAEAEGEKKADEGAEQKEGETDEVAALKKQLEAKDAEAREWKDKCLRTVADFRNLQERTARDVKQAKDFAIQKFAKDLVESVDNFERALSVVPQDKLKSEEQSEHLKDLVNLYEGLKMTESILLSTLKKHGLERIEPEGEVFNPNEHEATFMAPMPDKEHNVVFHVQQKGFKLNGRVLRPAQVGVVKNK

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.003 kDa

MSGDAPTPAHDPAAEGLEASVPLESVASMNSDEGQPSAQSAPLADNEARLQQLEQEHSSLREEHETLRSQYMRIAADFDNFRKRQSRDQDDLRLQLICTTLSEILPVVDNFERARQQLEPQGEEAQALHRSYQGLYKQLVEVLKQLGVASMRVVGQAFDPTLHEAVSREPSEEHPEDVVTEELQRGYHLNGRVLRHALVKVSMGPGPQSGASPSSAQSNDDSTATFQGEADPAEPGV

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.05 kDa

MSGDAPTPAHDPAAEGLEASVPLESVASINSDEGQSSAQSAPLADNEARLQQLEQEHSSLREEHETLRSQYMRIAADFDNFRKRQSRDQDDLRFQLICTTLSEILPVVDNFERARQQLEPQGEEAQALHRSYQGLYKQLVDVLKQMGVASMRVVGQVFDPTLHEAVSREPSEEHPEDVVTEELQRGYHLNGRVLRHALVKVSMGPGPQSGASPSSAQPNDDSTATFQGEADPAQPGV

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.003 kDa

MSGDAPTPAHDPAAEGLEASVPLESVASMNSDEGQPSAQSAPLADNEARLQQLEQEHSSLREEHETLRSQYMRIAADFDNFRKRQSRDQDDLRLQLICTTLSEILPVVDNFERARQQLEPQGEEAQALHRSYQGLYKQLVEVLKQLGVASMRVVGQAFDPTLHEAVSREPSEEHPEDVVTEELQRGYHLNGRVLRHALVKVSMGPGPQSGASPSSAQSNDDSTATFQGEADPAEPGV

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.05 kDa

MSGDAPTPAHDPAAEGLEASVPLESVASINSDEGQSSAQSAPLADNEARLQQLEQEHSSLREEHETLRSQYMRIAADFDNFRKRQSRDQDDLRFQLICTTLSEILPVVDNFERARQQLEPQGEEAQALHRSYQGLYKQLVDVLKQMGVASMRVVGQVFDPTLHEAVSREPSEEHPEDVVTEELQRGYHLNGRVLRHALVKVSMGPGPQSGASPSSAQPNDDSTATFQGEADPAQPGV

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.101 kDa

MTDSYKLPDNPGDPDATDDEGIHPDEVENLIEEAERTQGGSEDDDLLTTEPDPVVDAREDDRDPTLEEDLEGDLQAVLDDIDAELGVADTPEATGDLPTTEAQLAERTEDLQRVTAEYANYRRRTERERAGIIDTAKSGVVSKLLPILDDLDLAEQHGDLEEGPLKAFADKFRNTLTGLKVEAFGVPGDTFDPEIHEAVQDLSEGDTKVLGTVLRKGYRFNDKLIRNAMVIIADPEK

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.112 kDa

MPTEDAYPELQEEEIDVEAELEKLILEDREAEASTSSGEASAEASQDLSETLKQLQQELEITRQQLKEKEESYIRLYADFENYRRRTQREKEEFSQKERQKFVLEILPVVDSFERAQQQLKLETDREREVHNSYQSVYRLLVECLKKMGVSRMKSVGQPFDPNLHEAIARQPSSEYPEDVVAVEYQPGYKLGDLVIRHAMVAVSSGSPTSEPSPSDPATPKPEPESTPASPQNPQHS

grpE

Protein GrpE

237 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.792 kDa

MAPEDTYPELQEEEIDVEAELEKLILEDSEAEAGTSSGETAAEPSPDPGEALKQLQHELEVVRQQLKEKEDAYLRLYADFENYRRRTQREKEEFSQKERQKFVLEILPVVDSFERAQQQLKLETDRERELHNSYQSVYRLLVECLKKMGVSRMKSVGQPFDPNLHEAIARQPSPDYPEDVVAVEYQPGYKLGDLVIRHAMVAVSAGSPSSEPSPPAQATIEAGPENTPASPQNPQPS

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.559 kDa

MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTLGEQAESEPSGS

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.559 kDa

MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTLGEQAESEPSGS

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.559 kDa

MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTLGEQAESEPSGS

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

27.106 kDa

MENKNQKHNNEFHEKNQQSQKDNNNVKKENLHEDQSDLNDANFDDGGKKNKLKNDIKKLNHLVDSLKNENNNKQAKIESLERQINLLNENFKSEVIKKASEAQTKLDEKIKEFQAKYETELKHAKKYALKSSAIELIDIVSNFELAVNSKVTNPEIANYLKGFQMFANMFKNYFQQNGITEIPVNLNDDFNAEVMQAFETQKAPNTQPNKVIKIIKKGYKLHDIVLVPATVIVSE

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.533 kDa

MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTSGEQAESEPSGS

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.533 kDa

MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTSGEQAESEPSGS

grpE

Protein GrpE

235 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.533 kDa

MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTSGEQAESEPSGS

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.31 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.34 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDTIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.309 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADNFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.31 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.31 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.34 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDTIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.309 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADNFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

230 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.31 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEARAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

229 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.732 kDa

MSDFNKDDYLNDLPDADELANGQASPDADGADAPSDTGEQLKDDMLKDAAAEQSAGEQASEESAKAAAEATADAASDGDAEGSSLTPLGQAKKEAAEYLEALQRERAEFINYRNRTKKDMDRARQQGIIDVLTAMLPGLDDIDRIREHGEMDDSFKAVAAKIDKTFEKFGVEKFGLKGEDFDPTKHEAILHKPDPEASKATVDTVVEAGYRIGDRVIRAARVVVASPQN

grpE

Protein GrpE

229 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.248 kDa

MTEGNPHEQVTVTDKRRIDPDTGEVRSIPLGDTPGGSEPAGMTDRSANSTDTMVDKVAELTSDLQRVQADFANYRKRALRDQQTASDRAKATVISQLLGVLDDFDRAREHGDLDSGPLKSVADKLMSALTGLGLVAFGVEGEDFDPVLHEAVQHEGDGGEGSKPVIGDVLRHGYKLGDQVLRHALVGVVDTIAGDGAETVAIVAPVDSTAKTEQGELGDNVTPHKEDGD

grpE

Protein GrpE

228 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.97 kDa

MADEKNKSQNPDLEQRDINNPRDREALNRAADDFLKARKAEARAEVAEDEAEAAVDETANRIAMLEADNGELKDQLLRAAAEMENLRKRTQRDVQDARTYAVTNFARDMLSVSDNLRRALDAIPADALATDASLKSLADGVEMTERAMLQALERHGVKKLEPEGEKFDPNFHQAMFEVPNPDLPNNTVVQVVQDGYAIGDRVLRPAMVGVSKGGPKATADNGASEGNG

grpE

Protein GrpE

228 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.963 kDa

MDDKQKTNEEVKASSFDSEKSSKNQAFENTEEPAEGFQNVQHDNGSNPAQKQNSEAKEASKDQTNTNNNELSKKLEQLETERLTLQEKIAVLEQQHRELEEFLLKMKHEFALAKEALKRDQEKKERLLAESMARDLFPILDTLDHALEHDGENNGLRLIRSQLVSVLEKYGVVEVGKEGEVFDPNWHEFLGYAEGPENKIIKVVRKGYKIGDTLLRPALVVIGKESSC

grpE

Protein GrpE

227 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.709 kDa

MTQGNQKTEGNPPEQVTVTDKRRIDPETGEVRHVPPGDTPGGTAPQAATAESGGAATDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKAAVVNQLLGVLDDLERARKHGDLESGPLKSVADKLESALTGLGLTAFGEEGEEFDPVLHEAVQHEGDGSKPVIGTVMRQGYKLGDQVLRHALVGVVDTVTEEGDGEAAATDEPTAAAAETRPPESDDNAGASGD

grpE

Protein GrpE

226 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.883 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

226 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.883 kDa

MADEKNKPENPDLDQRDINNPRDREALKQAADDFLKARRAEAAADEAEGEVDETANRIAVLEADNTELKDQMLRVAAEMENLRKRTQRDVQDARAYAITNFARDMLSVSDNLRRALDAIPADALEADSNLKSLSEGVEMTERAMLLALERHGVKKLEPEGQKFDPNFHQAMFEVPNPDLPNNTVVQVVQAGYAIGDRVLRPAMVGVSKGGPKVSAENGASTSEDNA

grpE

Protein GrpE

226 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.685 kDa

MTPNDTENAARPLPEGAVDPAQDAAGAPDTLAPAAQADAVAALEAEKLDLKNKLLRALADMENLRRRTEREVADARTYAVTNFARDMLNVADNVRRALDSVPVEDRAAADGALKALLDGIELTGRDLAKTLERHGVRAVEPQGQRFDPNLHQAMFEVPNPDVANGTVVQVVQTGYVIGDRVLRPALVGVSKGGPKAAEASKPAGEAPKPAGEAPKPAGDGQKPAEA

grpE

Protein GrpE

225 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.874 kDa

MTEETPGFEEKPDVPSGATPDDAEPQAASEEGAAPAGDASENAGLVAQLDQVRTALNERTADLQRLQAEYQNYRRRVERDRVAVKEVAVANLLSELLPVLDDVGRAREHGELVGGFKSVAESLETTVAKLGLQQFGKEGEPFDPTIHEALMHSYAPDVTETTCVAILQPGYRIGERTIRPARVAVAEPQPGAQTVKPAEDAAEAQDSSGAEDDAGTKESGGPDEG

grpE

Protein GrpE

225 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.833 kDa

MSGDASTPEQDQNVVSGAVPATRESSPDAPEATSEQASAAVDPADRMQQLEQELSALKQEHDTLNSQYMRIAADFDNFRKRQSRDQDDMRKQLVCSTLTEILPVVDNFERARQQLNPEGEEAQALHRSYQGLYKQLVEVLKQQGVARMDVVGQEFDPNLHEAVLREESSEFAEDVVSEELQRGYHRDGRVLRHAMVKVSMGPGPSDPGSAPAEAAAAPDQTAEEA

grpE

Protein GrpE

224 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.077 kDa

MEKERDVAQEQATYEQESPNAERQEELKENEHQEKNAPEEQEKVREENGRQDAQKDEIGDPEKAKEEQNEELAAANAKIAELEAKIKEMENRYLRLYADFENFRRRTRREMEAAEKYRAQSLVSDLLPVLDNFERALKIKAEDEQAKSILQGMEMVYRSVLDALKKEGVEAIEAVGKPFDPHLHQAVMQVEDSNYEPNTVVEELQKGYKLKDRVIRPAMVKVSQ

grpE

Protein GrpE

224 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

26.077 kDa

MEKERDVAQEQATYEQESPNAERQEELKENEHQEKNAPEEQEKVREENGRQDAQKDEIGDPEKAKEEQNEELAAANAKIAELEAKIKEMENRYLRLYADFENFRRRTRREMEAAEKYRAQSLVSDLLPVLDNFERALKIKAEDEQAKSILQGMEMVYRSVLDALKKEGVEAIEAVGKPFDPHLHQAVMQVEDSNYEPNTVVEELQKGYKLKDRVIRPAMVKVSQ

grpE

Protein GrpE

224 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.86 kDa

MADNMDFKDLMADEAEDIIEKDIARVNQASEDIDQENQSEVVDDTTENEDASEEVYEEDTASEDGSKEKKSFFKKKEKKDKKDEKIDELTDRLMRNMAEFENFRKRTEKEKTQMFEVGAKDIIERILPVIDNFERGLAAVSVEEKDSAFVQGIEKIYKQLVTTLEAAGVKQIEAAGKEFDPDFHNAVMHAEDEEYGENIVAEEFQKGYMYRETVVRHSMVKVVN

grpE

Protein GrpE

224 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.129 kDa

MSGDASTSAQDQNVESNDVPAIPDVDAGTPIDPVVEETPTLDTEIDPANRLQQLEQELNSLKQEHEAVQSQYMRIAADFDNFRKRQARDQDDLRQQLVCSTLTEILPVVDNFERARQQLNPEGEEAQALHRSYQGLYKQLVDVLKQQGVARMEVVGQEFDPTLHEAVLREENQEHAEDIVCEELQRGYHRDGRVLRHAMVKVSMGPGPESSSDAASEQPQEGDA

grpE

Protein GrpE

222 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.835 kDa

MFDEKNKFTDASFENCDLKNPADRDTLKQAADELLKMHRGKEEVCADVEEEKNESTDLLATLQDENKELKDQFLRLAADMENLRRRTIRDVADAKIYSIANFARDMLSVSDNLNRALEAIPADARESDTNLKMLAEGVEMTERAMMAALEHHGVKKICPEGQKFDPNFHQAMFEISNSDVPDNTVQQVVQAGYIIGERVLRPAMVGVAKGGPKENSTEADSA

grpE

Protein GrpE

222 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.7 kDa

MSDEKNKFTDASFENCDLKNPADRNTLKQAADEFLKTHKTEAREDVEEESKEVDPLASLQDENKELKNQLLRLAADMENLRRRTARDVADARAYSIANFARDMLSVSDNLNRALEAIPEGARESDAGLKSLAEGVEMTERAMMAALERHGVQKIHPEGQKFDPHFHQAMFEIPNADVPDNTVQQVVQAGYIIGERVLRPAIVGVAKGGTKEASIETDKASHQ

grpE

Protein GrpE

222 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.856 kDa

MSDFNKDEYLNDLPDMDDLSGQAAPAAASADSAAAAAGATQEGAAQPAAAQSQENGDSAAADGADKAGAADGKADDTLTPLGQAKKEAAEYLEALQRERAEFINFRNRAQKEQERFRQHGIIDVLTALLPALDDIDRIREHSEMDDSFKAVANKIDKAFEKFGVEKFGEKGEDFDPTKHDAILHKPDPNAEKETVDTVVEAGYRIGDRVIRAARVVVASPQN

grpE

Protein GrpE

222 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.043 kDa

MNDGFAMNTHSKDERAPENGQAENMAVENGAEAAQAADRATPVSEEDVLLRLAKENEDLKERALRLTAEMENLRKRTQRDVADARVYGIANFARDMLTVSDNLQRALQAVSEEARAQADSGLKALVEGVEMTERAMLATLERHGVKRVDPNGEKFDPHFHQAMFEVPNADVPNNTVVQVVQPGYVIGDRVLRPAMVGVAKGGPKAETPAATSEQAAQGPEGA

grpE

Protein GrpE

221 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.608 kDa

MEQEQKATQEQATYEEWTAPEPQEEKAEERGGNEPQEENAENLQQENTQAQQEALEEQPKAEQEQNDELAAANAKNCRTRSEDKRNGNRYLRLYADFENFRRRTRQEMEAAEKYRAQSLVSDLLPALDNFERALKIETENEQAKSILQGMEMVYRSVLDALKKEGVEAIEAVGKPFDPHLHQAVMQVEDSNYEPNTVVEEFQKGYKLKDRVIRPAMVKVSQ

grpE

Protein GrpE

221 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.608 kDa

MEQEQKATQEQATYEEWTAPEPQEEKAEERGGNEPQEENAENLQQENTQAQQEALEEQPKAEQEQNDELAAANAKNCRTRSEDKRNGNRYLRLYADFENFRRRTRQEMEAAEKYRAQSLVSDLLPALDNFERALKIETENEQAKSILQGMEMVYRSVLDALKKEGVEAIEAVGKPFDPHLHQAVMQVEDSNYEPNTVVEEFQKGYKLKDRVIRPAMVKVSQ

grpE

Protein GrpE

221 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.316 kDa

MTDKNVNPDDDQADENRDDNVDERFADIVGDVDIDADQSATDSPAPEELSRESQLEALLAERTEDLQRLQAEYVNYKRRVDRDRALSRQSGVDKVITDLMPVLDSIAMARQHGEVEGGFKLVVDELEKVANNHGLTSFGEVGDVFDPNLHEALMQMPMEGVSVTSVSQVMQPGYKLGDRVLRPARVAVSDPDPNATSADESSQADGESAQADEDDETPRNE

grpE

Protein GrpE

221 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.724 kDa

MFTNPFGRKKDMSDDQKKNNQPDTEADNAENIKFAADDTELRAGDETDADFEMPEGFPEMDENMFGQVQEMMAKLERVDELEKENADLKNRLGRLASDFEGYRNRTTIESAEAHDKGVSKAAEALMPVYDDIDRALSLSVDDAAKLVPGMQAVQNKVLTIFGTLGLEATGREGEQFDPQWHEAIQVVAGDEDEKIVQTYQLGFKMGDRLVRPARVVVSRKG

grpE

Protein GrpE

220 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.207 kDa

MCGGDVQGQGVASGCDEALERADSLRASDPVPVESGEGSVPGEHSQELETGASEETLRERVNVLQEQYLRKAADLENYRKRALRERQEAVEHAYAALLADIVAVLDDFDRAIEAADHASSTEVEASSAFREGVLMIRKQLSSVLETKYGLEYYPVLGERFDPNLHEALSMSPSASVHEKIVGAELQKGYRVRNRILRHAKVMVLTPEEQTEPDRGDGPSE

grpE

Protein GrpE

220 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.207 kDa

MCGGDVQGQGVASGCDEALERADSLRASDPVPVESGEGSVPGEHSQELETGASEETLRERVNVLQEQYLRKAADLENYRKRALRERQEAVEHAYAALLADIVAVLDDFDRAIEAADHASSTEVEASSAFREGVLMIRKQLSSVLETKYGLEYYPVLGERFDPNLHEALSMSPSASVHEKIVGAELQKGYRVRNRILRHAKVMVLTPEEQTEPDRGDGPSE

grpE

Protein GrpE

220 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.611 kDa

MEQGDKQATYNELETEQPVSKEGADSQPEDEAIGAASEHADAQAGENPEAASTTADPAEQTSVEAEELAKAKAQVAELEEKLAEMEKRYLRLYADFENFRRRARQEMEAAEKYRAQSLASDLLPVLDNFERALKIETENEQAKSILQGVEMVYRSLLDALRKEGVEVIEAVGKPFDPHLHQAVMQTDEGGYEPNTVVEELQKGYKLKDRILRPAMVKVSQ

grpE

Protein GrpE

220 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.925 kDa

MSDEKNKFTDASFENCDLKNPSDRDALKQAADKFLKAHAAEADADVKGGGEALVDPLAALQDENKELKDQLLRLAADMENLRRRTARDVADAKAYSIANFARDMLSVSDNLNRALDAIPEGAKENDAGLKTLAEGVEMTERAMIAALERHGVQKIHPEGQKFDPHFHQAMFEIPNSDVPDNTVQQVVQAGYIIGERVLRPAIVGVAKGGAKDISVESDSD

grpE

Protein GrpE

220 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.348 kDa

MSDEKNKFTDASFENCDLKNPVDRDTLKKATDEFLKTHEAEIHSEVKEENNEVSDPLAALQDENKELKDQLLRLVADMENLRRRTARDVADAKAYSIANFARDMLSVSDNLNRALEAIPEGAKENDAGLKTLAEGVEMTERAMIAALERHGVQKIYPEGQKFDPHFHQAMFEIPNCDVPDNTVQQVVQAGYIIGERVLRPAIVGVAKGGTKGVPVESGSA

grpE

Protein GrpE

219 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.89 kDa

MSTTDNTNGDDRRPGQPEWDDEENNFEHLDATEVPAEEEALVESAGLDADTLADLEDAFDGVDASTEDPGATVGETSTLESELAERTEDLQRLSAEYANYRRRTDRERKVGVEAAKAKVLGELLPILDDLELAQKHGDLDEGPLKAFRDKLVSVVEGLGVSAFGAEGDVFDAERHEAVQDLSSGDDKVLGTVLRRGYQMNDRLLRTAMVIIADPAEDAQ

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.637 kDa

MSKNNENIKHQNNDKVNNQVDKKETKNHNKQEFKYKELYEHELKKNKELQNINTLLKDKNQQLEEQISQLNQDFIKQLETKAKQAQQILEQKVNELEARHEAKVNDAVFKIFKFKMEPLLDAINHFTKIVNQNYDDPKIQAFIEGFKMFSQNMIDGLDNLKITKISPQVNDSLNDEIMEVFEVVENTNKPSMHVVEVISDGFKYNDKVIKFAVVKVAK

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.637 kDa

MSKNNENIKHQNNDKVNNQVDKKETKNHNKQEFKYKELYEHELKKNKELQNINTLLKDKNQQLEEQISQLNQDFIKQLETKAKQAQQILEQKVNELEARHEAKVNDAVFKIFKFKMEPLLDAINHFTKIVNQNYDDPKIQAFIEGFKMFSQNMIDGLDNLKITKISPQVNDSLNDEIMEVFEVVENTNKPSMHVVEVISDGFKYNDKVIKFAVVKVAK

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.532 kDa

MKEKNSNKINEDKLNKKSEVKNKKEEEIINNKKQTTEKKINLNKNNISDEIIPEKINFNDQKNIIENLKKNLSKEKKSKHDLILRNQAEMENLMKRTQANIEKSYKFALEKFSIALLPIIDNLERTKNLLEKENEKNKNINPIEEGINLTLKEFIKVIHSFGIKEIDKKNIPFDPKIHEAMTVIDDKNKKTNQVVEIMQKGYILNGRLLRPAMVVVSK

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.637 kDa

MSKNNENIKHQNNDKVNNQVDKKETKNHNKQEFKYKELYEHELKKNKELQNINTLLKDKNQQLEEQISQLNQDFIKQLETKAKQAQQILEQKVNELEARHEAKVNDAVFKIFKFKMEPLLDAINHFTKIVNQNYDDPKIQAFIEGFKMFSQNMIDGLDNLKITKISPQVNDSLNDEIMEVFEVVENTNKPSMHVVEVISDGFKYNDKVIKFAVVKVAK

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.637 kDa

MSKNNENIKHQNNDKVNNQVDKKETKNHNKQEFKYKELYEHELKKNKELQNINTLLKDKNQQLEEQISQLNQDFIKQLETKAKQAQQILEQKVNELEARHEAKVNDAVFKIFKFKMEPLLDAINHFTKIVNQNYDDPKIQAFIEGFKMFSQNMIDGLDNLKITKISPQVNDSLNDEIMEVFEVVENTNKPSMHVVEVISDGFKYNDKVIKFAVVKVAK

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.532 kDa

MKEKNSNKINEDKLNKKSEVKNKKEEEIINNKKQTTEKKINLNKNNISDEIIPEKINFNDQKNIIENLKKNLSKEKKSKHDLILRNQAEMENLMKRTQANIEKSYKFALEKFSIALLPIIDNLERTKNLLEKENEKNKNINPIEEGINLTLKEFIKVIHSFGIKEIDKKNIPFDPKIHEAMTVIDDKNKKTNQVVEIMQKGYILNGRLLRPAMVVVSK

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.676 kDa

MTTPNGMPDNPGDPENTDPEATSADRAEQAAEEAAARQAEESPSGQALEEEISPELEAEINDLLSDVDPDLDGDGEVSAVETQLAERTEDLQRVTAEYANYRRRTERERQGIIDTARASVVTQLLPLLDDLDLAEQHGDLNEGPLKSLSDKLINILGGLKVESFGEIGEAFDPEIHEAVQDLSQGDVKVLGTVLRKGYRLGDRVIRTAMVLIGDPEES

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.68 kDa

MTTPNGMPDNPGDPENTDPEATSADRAEQAAEEAAARQAEESPFGQASEEEISPELEAEINDLLSDVDPDLDGDGEVSAVETQLAERTEDLQRVTAEYANYRRRTERERQGIIDTARAGVVTQLLPLLDDLDLAEQHGDLNEGPLKSLSDKLINILGGLKVESFGEIGEAFDPEIHEAVQDLSQGDVKVLGTVLRKGYRLGDRVIRTAMVLIGDPEES

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.57 kDa

MSEFNKDDYLNDLPDPSDAEAAAQASSGADASAESGSAQDSAAQAPSNEGADAAPAAAEGEKTGEGQSDSADTLTPLGKAKKEAADYLEALQRERAEFINYRNRTQKEQERFRQHGIIDVLTALLPALDDIDRIREHSEMDDSFKAVATKIDKAFEKFGVEKFGEKGEDFDPTKHDAILHKPDADAEKETVDTVVEAGYRIGDRVIRAARVVVASPQN

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.955 kDa

MSDKQREAERQQSEDKAHSEAESAEAGQAPEAQAAEDGAESASGDSGDELTELQQALEEARARAEENWNECLRARAEMQNIQRRAQADVEKARKYAVEKIAGDLLGVKDSLEMGVKAAKEEGADPQKLLEGSELTLKMLSQVLERFNVQEIDPQGERFNPEHHEAVAAQPSHEHEPNTVLNVMQKGYALHDRVLRPAMVVVSQKAPEPPPSGSIDEQA

grpE

Protein GrpE

218 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.227 kDa

MSGEASTPAQDPSVEPLDAAPVAAEPEVMSTETPAEGSLTDPAERLQQLEHELQTLKQEHETLQSQYMRIAADFDNFRKRQSRDQEDIRQQLVCSTLSEILPVVDNFERARQQLNPESEEAQALHRSYQGLYKQLVDVLKQQGVARMEVVGQLFDPTLHEAVLREESTEQPEDVVIEELQRGYHLNGKVLRHALVKVSMGPGPSADAEGAASAEAEDS

grpE

Protein GrpE

217 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.863 kDa

MSDHAEHAADAADTDAPEGDDAGGDDGEQAGDDGTSALSERVRALDADNADALADDVAALEARVETLTDELADAEDEVADLTERVQTKQADFKNYKERAKRKQEEIRERATEDLVERLLDVRDNLDRALDQEESESDEDGIREGVELTRDEFDRVLETEGVTEIRPEPGDSVDAARHEVMMRVDSDQPAGTIVDVYRPGYEMSGRVVRAAQVTVSEE

grpE

Protein GrpE

217 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.863 kDa

MSDHAEHAADAADTDAPEGDDAGGDDGEQAGDDGTSALSERVRALDADNADALADDVAALEARVETLTDELADAEDEVADLTERVQTKQADFKNYKERAKRKQEEIRERATEDLVERLLDVRDNLDRALDQEESESDEDGIREGVELTRDEFDRVLETEGVTEIRPEPGDSVDAARHEVMMRVDSDQPAGTIVDVYRPGYEMSGRVVRAAQVTVSEE

grpE

Protein GrpE

217 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

25.014 kDa

MCEKSQTIKELLNAIRTLVVKNNKAKVSMIEKELLAFVSELDKKFKQQLNNFNELQQKIPLLQKANEEFALKFERMQREAQNQIQAKLDELNLKNKKELEQAKKYAIAKTLDQPLNIIDQFEIALSYAQKDPQVKNYTTGFTMVLDAFSRWLEANGVTKIKIEPGMEFDEKIMSALELVDSNLAKNKVVRVSKSGYKLYDKVIRFASVFVSKGNKKS

grpE

Protein GrpE

217 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.706 kDa

MSENSLTITEILSSIRTLLVKHNKAKVTQIEKELLQAVAELEKKFKQQVQNFNELQQKIPNLQKVNEEFRLKVEKIQEEAQKKIQEKVAELTIKSKEELENAKKYVIEKSIDQPLIIIDQFEIALSYAQKDPQVKNYTTGFNMVLDAFSRWLEGFGVTKIAIEPGAQFDEKVMAALEVVPSDQPANTVVKVSKSGYKLHDKVIRFASVVVSQGNKTE

grpE

Protein GrpE

217 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.817 kDa

MSDDQGDAVEASSEADEEASTSPDEGDDRDPVAAVAERAENDPASVAAELVALREEAAELETERDDLESRLKRKQAEFQNYKKRQEKQREKERARATEALVEKLLEVRDNLNRALEQDADADIREGVEATFRQLDDILDGEGVEAIEPDPGTETDPKRHEVLLQVESDEPEGTVAELHRPGYEMAGKVLRAAQVTVSEGPSGDSEAEDDADGEDGDE

grpE

Protein GrpE

216 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.223 kDa

MTEETPGFEEKPDVPSGATPDDAEPKAADSSEEETAAPAGDLDPTVGLTAQLDQARTALGERTADLQRLQAEYQNYRRRVERDRVTVKEIAVANLLSELLPVLDDVGRARDHGELVGGFKSVAESLETTVAKLGLQQFGKEGEPFDPTIHEALMHSYAPDVTETTCVAILQPGYRIGERTIRPARVAVAEPQPGATPAAAKEEKTDDEESGGTEEV

grpE

Protein GrpE

215 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.084 kDa

MKHTSDTPSNSDMPSDSQATQPNASATGQAAHAYSSQAQRASADAQAVAGDEAAVAEAVADVDVAELRRQLEAAEEKARQNYENWARATAEGENIRRRGQDDVAKAHKFAIEGFAEYLLPVMDSLQAALADTSGDATKLREGVELTLKQLYAAFEKGRVTELNPVGEKFDPHRHQAISMVPADQEANTVVAVLQRGYTLADRVLRPALVTVAAPK

grpE

Protein GrpE

214 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.889 kDa

MKHTSEPTSQPDTQAAESAQSSAAAAGQAASAYSSQAQRASADAQAIAGDEAAVAEATIEPDTAELRRQLEAADEKARQNYENWARAVAEGENIRRRAQDDVARAHKFAIEGFAEYLLPVMDSLQAALADASGDVAKLREGVELTLKQLNAAFEKGRVTELNPVGEKFDPHRHQAISMVPADQEANTVVNVLQRGYTLADRVLRPALVTVAAPK

grpE

Protein GrpE

213 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.044 kDa

MEQGEKQVMEQATYDEPEREQPIEEEAAPQPEEESGGVPLEEAGGEEAAEPAEKAPTAEELAAAKAQIAELEAKLSEMEHRYLRLYADFENFRRRTRQEMEAAEKYRAQSLASDLLPVLDNFERALKIETDNEQAKSILQGMEMVYRSLVDALKKEGVEAIEAVGKPFDPYLHQAVMQAEAEGYEPNTVVEELQKGYKLKDRVLRPAMVKVSQ

grpE

Protein GrpE

213 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.044 kDa

MEQGEKQVMEQATYDEPEREQPIEEEAAPQPEEESGGVPLEEAGGEEAAEPAEKAPTAEELAAAKAQIAELEAKLSEMEHRYLRLYADFENFRRRTRQEMEAAEKYRAQSLASDLLPVLDNFERALKIETDNEQAKSILQGMEMVYRSLVDALKKEGVEAIEAVGKPFDPYLHQAVMQAEAEGYEPNTVVEELQKGYKLKDRVLRPAMVKVSQ

grpE

GrpE protein homolog, mitochondrial

213 amino acids

Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity).

Belongs to the GrpE family.

24.585 kDa

MNSLIRRGLVSIRTSTVIKPSSFGLMRNNRFYSTENNQEAAKPEETENKPAPGSLEETIEKLKEELEETKKQLLYTAADRENVRRFAKEDNEKAKKFGIQSFTKELLEVVDQLEMATNLFPKEKLDENKELKDLHEGVKMTEQLFLKIMGNQGLQRFNPIGEKFDFNNHHAIFELNDPTKENNTVGHVVKQGYKLHDRLVRPAMVGVNKIKPQ

grpE

Protein GrpE

213 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.138 kDa

MSDEKKPEAETSESLQKREEKLAETLASEPAAQGEAEDAAAAGPDVAALEAEISDLRNRLLRAAADMENNRKRAEREKQDAQRYAAANFARDMLEVSDNLRRAIATLKEDERAEAAESVKAMIEGVEMTDRQLVTIFERHGIREITPQPGERFDPNLHEAMFEVPGTDQPAGTVVHVLGAGYMIGDRLLRAARVGVAKADDGAAKGGKVDTIA

grpE

Protein GrpE

211 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.718 kDa

MFVKQKSGGKKLEEKNNQENIENQEQNQEEVREEKPLTEQEKDELIKKLQEEVETLKQKLQKTEEAAKRLSALYQSIQKDFEDYKIRAIKEREQIKEESIEKFAKAFLDVVDNFEKALESFKVSNDINAIMQGIRMTHYQIMNLLQSYGIEKIEAAGEFNPMEHEALETLKTKEYRNNQIVKVLQAGYKYKGKVIRPAKVVVAISEEEEIT

grpE

Protein GrpE

211 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.934 kDa

MTDETTKNGPDATAADAAADAAANVEIDNSVQEEAKQPDPLELLKAENAELRDRYLRLAAEMDNLRRRTEREVKDAKSYSVAGFARDMLAVSDNLRRALDAISPEAKATADAGLTTLIEGVEMTERSMLSALERHGVRKLEPVGQKFDPNFHQAMFEVPNSEVPNNTVVQVVQAGFTIGERVLRPAMVGVAKGGPKPVEAEINSVFDEKDA

grpE

Protein GrpE

211 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.831 kDa

MTDDTKKPGPDADVAEEFVDPAQAGEEQAETAEPDPVELLKAENADLRDKFLRLAAEMDNLRRRTERDVKDAKAYSLAGFARDMLAVSDNLRRALEAIPDELKTNGEAGLNGLIEGVEMTERSMLSTLERHGVKKIDAEGQKFDPNFHQAMFEVPNTAVPNNTVLQVIQAGFTIGDRVLRPAMVGVAKGGPKAEPSASAEPGTSSLNEKDA

grpE

Protein GrpE

211 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.831 kDa

MTDDTKKPGPDADVAEEFVDPAQAGEEQAETAEPDPVELLKAENADLRDKFLRLAAEMDNLRRRTERDVKDAKAYSLAGFARDMLAVSDNLRRALEAIPDELKTNGEAGLNGLIEGVEMTERSMLSTLERHGVKKIDAEGQKFDPNFHQAMFEVPNTAVPNNTVLQVIQAGFTIGDRVLRPAMVGVAKGGPKAEPSASAEPGTSSLNEKDA

grpE

Protein GrpE

211 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.094 kDa

MVDKDEEQIKQNVEEDLSSTVEQTGEENIEFPSAPNHPKQVLVTDEELKALKKEATEYKDKYLRLLADSENARKRLQKERQEISRYALENMVVDFLKPLDNLENALKFAQGMSDEVKNWAFGFQMILTQFKDVLASNGITALESQGTFFDPHLHEAIEMVETDSYAPGIIVEENVRGYKMGDRMIRPARVKVAKAISAIDPQDKSELNENN

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.248 kDa

MANEERTIPETNVASERPEDPVESQTRAEGGEQIQEAAPETAELEAVQQLLEDARSKADEHWNELLRARAELENQRRRHERELEKGRKYALEKFAQDLLPVKDSLEMGLAAAQAEDANVTALREGTELILKMFNEVAARFGIETIDPQGEAFNPDFHQAISTQESSEAAPDTVLTVVRKGYALNGRLLRPAMVVVSKPGEQTTAGVDTQA

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.802 kDa

MTDETTKNGPDATAADAAADAAAYVENDTVQEETAQPDPLELLKAENSELRDRYLRLAAEMDNLRRRTEREVKDAKSYSVAGFARDMLAVSDNLRRALDAISPEAKATADAGLTSLIEGVEMTERAMLSALERHGVRKLEPVGQKFDPNFHQAMFEVPNSEVPNNTVVQVVQAGFTIGERVLRPAMVGVAKGGPKPAEAETNSVFDEKDA

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.795 kDa

MTDDTTKNGPDATAADAAADATAYVENETAQQEPAQPDPIELLKAENGELRDRYLRLAAEMDNLRRRTEREVKDAKSYSVAGFARDMLAVSDNLRRALDAISPETKATADAGLSTLIEGVEMTERAMLSALERHGVRKLEPVGQKFDPNFHQAMFEVPNPDVPNNTVVQVVQAGFTIGERVLRPAMVGVAKGGPKPAEAETNSVFDEKDA

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.741 kDa

MSDQAKDERAPSEAEAAEANAERTEGSIDGDYEALVRLLKENEELKDRALRVAAEMENLRRRTARDVHDARTYAVANFARDMLSVSDNLRRALDAIPAEAKASGDAGFKALIEGVDLTERAMLSALERHGVKKLAPEGEKFDPNFHQAMFEVPNPDVPANTVVQVVQPGYSIGERVLRPAMVGVAKGGPKIAAEAPVEPGPVNEQAEKDA

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.694 kDa

MTDDTTKNGPDATAADAAADAAAYVENDIAQEEAPQPDALELLKAENGELRDRYLRLAAEMDNLRRRTEREVKDAKSYSVAGFARDMLAVSDNLRRALDAIPAEVKDAADAGLSTLIEGVEMTERAMLSALERHGVRKLEPVGQKFDPNFHQAMFEVPNPDVPNNTVVQVVQAGFSIGERVLRPAMVGVAKGGPKAAEAETNSVFDEKDA

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.911 kDa

MAKDPQTPTDEELARAERDAEPQPGDATDDEVELEGVVEDVEASEADAEALENPEADALAARVEELEQALADAKDQTARAAAEAQNVRRRAEQDVEKARKFALEKFVKELLPVVDSLEKALESMQEGASEVHREGVSMTLKLQLDVLAKFGVEAVDPQGEPFDPQVHEAMTMVPNPEVEPNTVIEVMQKGYLLNGRLVRPAMVVVSQAAN

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.035 kDa

MSEKDQSVNNTEEDFNVETEDNQNDTNIENSVSNTDNSEANASDSENNSEESIKDEESESQDTKIKELEKLANDNEEKYLRLYAEFENYKRRIQKENQINATYKAQGVLTDILPSIDNIERALQIEGDDESFKSLQKGVQMVHESLLRALKDNGLEEILAEGKEFDPNLHQAVVQDDNPDFKSGEVTQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

210 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.035 kDa

MSEKDQSVNNTEEDFNVETEDNQNDTNIENSVSNTDNSEANASDSENNSEESIKDEESESQDTKIKELEKLANDNEEKYLRLYAEFENYKRRIQKENQINATYKAQGVLTDILPSIDNIERALQIEGDDESFKSLQKGVQMVHESLLRALKDNGLEEILAEGKEFDPNLHQAVVQDDNPDFKSGEVTQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.935 kDa

MTTESTSNKEELSAEQLADDIVQQAEEQVEDQHDHAHEVISAEQEKINELELALATAQSTVADQKDSVIRAKAEVDNIRRRAAQDVEKARKFALEKFAGEMLTSVDNLERALQNIDKEDESNKGVIEGVELTLQGLITSLDKFGVKAVDPQDQPFNPELHQAMSMQEVPGVAPNTVIAVMQKGYELNGRLIRPAMVMVSKAAPTVDATA

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.405 kDa

MKKSTKKESTHSKEESQTQAGNSEARKSGPSTKKAGEKTAEPEKATAGSGTEKSPEAACREENELLKDQLFRLAADFDNFKKRTARQMEENRKAVLEQVLLDFVEVTDNFERALKSAQTAEDMGSIVSGIEQLSKQFFSILQKYGLERIKCEKAGEFDPHRHEAVQHIETSEVPDNTIVDVYKPGYSLNEKVIRPALVSVARNPDETEK

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.598 kDa

MKIFNKDGNKNSKEDTKAGAENSEAQNSGSSAEEVNKARENPEEASASSEAEKSPEVKCQEEKQVLMEKYYRLAADFDNFKKRTARQMEENRKAVLEQVLLDFVEVTDNFDRALKSAKTAEDMSSIVSGIEQLSRQFFSILEKYGLEKIESEKASEFDPHRHEAVHHIETSEVPDNTIVDVYKTGYALNSKVIRPAMVSVARNPDEAEK

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.995 kDa

MKKSRKKENMDSKERNQKEAERSEARNSESPAEKAGETKVSPENEPSSPEAEKNPEEACREENEILKDQLFRLAADFDNFRKRTARQMEENRKSVLEQVLLDFVEVTDNFDRAIKSARTAEDMGPIVSGIEQLSKQFFSILEKYGLERVKCEKAGEFDPHRHEAIHHIETSEVPDNTIVEIYKEGYALNEKVVRPALVSVARSPEEAEK

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.995 kDa

MKKSRKKENMDSKERNQKEAERSEARNSESPAEKAGETKVSPENEPSSPEAEKNPEEACREENEILKDQLFRLAADFDNFRKRTARQMEENRKSVLEQVLLDFVEVTDNFDRAIKSARTAEDMGPIVSGIEQLSKQFFSILEKYGLERVKCEKAGEFDPHRHEAIHHIETSEVPDNTIVEIYKEGYALNEKVVRPALVSVARSPEEAEK

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.885 kDa

MSNDSSKAKQNQVDEAVEGEIITDNENETVTGEASLMDELTQANFRVEELEQALEAATAKVDEQKDSVIRAAAEVDNIRRRAAIDVEKARKFALEKFANELLPVIDNMERALQGTDAEAEATKAVYEGVELTLKSFIGTVEKFGLTVVNPQGETFNPEHHQAIGMQPSPDFPANTVMMVMQKGYILNERLLRPAMVMVSQGGAAVDTQA

grpE

Protein GrpE

209 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.982 kDa

MSNDSSKAKQNQVDEAVEGEILTESEVETGNDEASLMDELTQANFRVEELEQALAEANAKIEEQKDSVTRAAASEANIRRRAAQDVEKAHKFALEKFANELLPVIDNMERALQGTNAEAEETKAIYEGVELTLKSFVSTVDKFGLKEVNPHGESFNPEHHQAIGMQPSPEFPANTVMMVMQKGYILNDRLLRPAMVMVSQGGSGVDTQA

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.362 kDa

MTDETNKNGPEAAAPEEFETAAEPQAAEKPEADASTTAPDPLELARAESAELRDKYLRLAAEMDNLRRRTERDVKDAKSYSVAGFARDMLAVSDNLRRALDAIPADAREAGDAGLKALIEGVEMTERSMLAALERHGVKQLDPTGQKFDPNFHQAMFEVPNTEVPNNTVVQVVQAGYTIGERVLRPAMVGVAKGGPKAATSESETPAA

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.201 kDa

MVDNKDFNEELKENIQEELDNETKAENPNIDEEVEEVSEDIKADEKVIDFEELKALKEENTMFKSKTKKLENELEALKDRLLRISAEYENYRKRTDKEKERIYTDACEDVLIKMLPVLDNLERALAVDGTVEDLKKGVEMTVRQFEDALEKLQVEEISTENGFDPELHQAMMVVEQEGAEPNQVAQVFQKGYKRGDKVIRHSMVTVTK

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.201 kDa

MVDNKDFNEELKENIQEELDNETKAENPNIDEEVEEVSEDIKADEKVIDFEELQALKEENTMFKSKTKKLENELEALKDRLLRISAEYENYRKRTDKEKERIYTDACEDVLIKMLPVLDNLERALAVDGTVEDLKKGVEMTVRQFEDALEKLQVEEISTENGFDPELHQAMMVVEQEGAEPNQVAQVFQKGYKRGDKVIRHSMVTVTK

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.222 kDa

MVDNKDFNEELKESIQEELDNETKSENPNIDEEVEEVSEDIKADEKVIDFEELKALKEENTMFKSKTKKLENELEALKDRLLRISSEYENYRKRTDKEKERIYTDACEDVLIKMLPVLDNLERALAVDGTVEDLKKGVEMTVRQFEDALEKLQVEEISTENGFDPELHQAMMVVEQEGSEPNQVAQVFQKGYKRGDKVIRHSMVTVTK

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.294 kDa

MTDETNKNGPEAAAPEEFDAAAQPETAEEPEADVSAAAPDPLELAKAENAELRDKYLRLAAEMDNLRRRTERDVKDAKSYSVAGFARDMLAVSDNLRRALDAIPADAREAGDAGLKALIEGVEMTERSMLAALERHGVKQLDPTGQKFDPNFHQAMFEVPNPEVPNNTVVQVVQAGYTIGERVLRPAMVGVAKGGPKAASSEGETPPA

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.022 kDa

MTNKDESVEKNTESTVEETNIKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.022 kDa

MTNKDESVEKNTESTVEETNIKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.022 kDa

MTNKDESVEKNTESTVEETNIKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEVTNVKQNIDDSVEQTEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.007 kDa

MTNKDESVKKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.022 kDa

MTNKDESVEKNTESTVEETNIKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.022 kDa

MTNKDESVEKNTESTVEETNIKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.707 kDa

MERMNQSRKVPIHDAAEESSAEAHETQEAGNMEEQAREAEIQQEMAEEAVEQAQDAEEAQEEEAADYKDLYLRTLAEFENYRRRADRETNEFKKYANETLIKDIIPVIDNLERAMECTVNTDDPGCAQNLLAGVQMTEREILKVLEKYGVTRISAIGETFDPAYHQALMAEESDEHPDETVIREMQKGYLLKDRLIRPALVAVAKGKA

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.022 kDa

MTNKDESVEKNTESTVEETNIKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.008 kDa

MTNKDESVEKNTESTVEETNVKQNIDDSVEQAEESKGHLQDEAIEETSDENVIEEIDPKDQKINELQQLADENEEKYLRLYAEFENYKRRIQKENEINKTYQAQRVLTDILPAIDNIERALQIEGDDETFKSLQKGVQMVHESLINALKDNGLEVIKTEGEAFDPNIHQAVVQDDNPDFESGEITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.979 kDa

MTEKDESVKSNSEYTEEQEVKNEDTSTVENVEDTTSDSDNSSNDSSNEESSEETAVDPKDEEIQQLQLKANENEEKYLRLYAEFENYKRRIQKENETNKTYQSQRVLTDILPTIDNIERALQIEGDDESFKSLQKGVQMVHESLLRALKDNGLEEIESEGQAFDPNFHQAVVQDDNPDFKSGDITQELQKGYKLKDRVLRPSMVKVNQ

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.017 kDa

MTDEQTPAEEMPFEADDAAQEIEALKLEVAQLKEQALRYAAEAENTKRRAEREMNDARAYAIQKFARDLLGAADNLGRATAHSPKDSTDPAVKNFIIGVEMTEKELQSAFERNGLKKIDPAKGDKFDPHLHQAVTEQPSTEVAAGGVLMVMQAGYELMGRLVRPAMVAVAAKGSTGPASPDAPAASANPYAGAAAEGDSTGGAFDAKA

grpE

Protein GrpE

208 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding (By similarity).

Belongs to the GrpE family.

22.017 kDa

MTDEQTPAEEMPFEADDAAQEIEALKLEVAQLKEQALRYAAEAENTKRRAEREMNDARAYAIQKFARDLLGAADNLGRATAHSPKDSTDPAVKNFIIGVEMTEKELQSAFERNGLKKIDPAKGDKFDPHLHQAVTEQPSTEVAAGGVLMVMQAGYELMGRLVRPAMVAVAAKGSTGPASPDAPAASANPYAGAAAEGDSTGGAFDAKA

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23 kDa

MSEHQTPPEEDLTVANGDSAEAVSEPDVTVASGQEAAELAAQLALVAADRDRLKTELDEQNSAYLRLAADFENFRRRTLKEREELELQSKRTTITELLPVIDNFDRARAQIKPQGEEAEAIHKSYQGLYKQLVDCLKRIGVSPMRAEGQPFDPSLHDAVLREETTEHPDGIVLEELQRGYLLGDLVLRHALVKVSIAAEENSAAVTE

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.964 kDa

MTDPNGPKDIPEQSAEAAEPVVSKPYIMPDDPEPDAVELLAKEAAEARDKMLRTLAEMENLRKRTTREVADARIYGVTAFARDVLEIADNLQRALDAVPAEARANAEPGLKALIDGVELTERSLINALEKNGVKKFDPSGQKFDPNFQQAMYEVPDASVPAGTVVQVVQAGFMLGERVLRPALVGVSKGGAKAAPAAAANGESNSAA

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.076 kDa

MTETDGQKDNNQDTAQAAADPVVSKPYIMPDDPEEGSNEALVREAADARDKMLRTLAEMENLRKRTQKEVADARTYGVTSFARDVLDIADNLQRALDAVPADARANAEPGLKALIEGVELTERSLLNALEKNGVKKFDPKGQKFDPNFQQAMYEVPDPSVPAGTVVQVVQAGFTIGDRVLRPALVGVAKGGAKAAPSDGGGETGNLN

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.12 kDa

MTETDGQKDNNQDTAQAAADPVVSKPYIMPDDPEEGSNEALVREAADARDKMLRTLAEMENLRKRTQKEVADARTYGVTSFARDVLDIADNLQRALDAVPAEARANAEPGLKALIEGVELTERSLLNALEKNGVKKFDPKGQKFDPNFQQAMYEVPDPSVPAGTVVQVVQAGFTIGDRVLRPALVGVAKGGAKAAPSDGGSETGNLN

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.564 kDa

MEENRDVKNEELEKEEIADEVAEKDNETQESNDAAETNEASKEASENIEAAEEDQEDLVKNQEEENKKLREELDATKDRLLRLTAEYDNYRKRTAKEKEGIYSDAYVDVLKEIVPILDNLERAVAADGSIEDLKKGIEMTIKGCKDSFAKLGVEEIDATGEFDPNLHNAVMHIEDEELGKNVVAEVFQKGYKKDDKIIRHTMVKVAN

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.456 kDa

MSNEERKERGHEPEGPQREEKVEEPQGSPVDPASVEENAPPEASAETAPEEAGKEVREEELAKLREELEAVRRERDEYLDALRRLKAEFENSRKRMEREAQRIREAAAERLVAELLPVLDNLDRALEAEGDIREGVRATRDQLTDVLSREGLTPIASDGQHFDPSVHEAVMSQPSEEHEEGTIIQTFERGYMFNGRPIRPAKVVVAV

grpE

Protein GrpE

207 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.669 kDa

MTKKVMDEQESHKEYLDEILQAGEVQEDTVPLVEWSQGQSSPEGECTEARIAELETELARQKEQAGKYRDELLRRAADFENFRKQKEREAMMASSRALENIIRELLPVIDDVKRLLDHAPLSAERSSEARPYIEGVEMVKKNLEKWLDEKGVKAIASIGTMLDVNFHEAISQIDSPDAEPDMIVDEYQTGYLLGERVIRHAKVIVAR

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.097 kDa

MTDPDLHQNDPENPAQASEPVVSKPYIMPDDPETGSAEAYAKEAAEARDKMLRTLAEMENLRKRTAREVADARMYGITGFARDVLDIADNLQRALDAVPAETRANADAGLKSLIEGVELTERSLLNTLEKNGVKKFDPTGQKFDPNFQQAMYEVPDPSVPSGTVVQVVQAGFMIGERVLRPALVGVSKGGAKAAPAASNDQSNSAA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.557 kDa

MSKKASMHKEEKHEKGQHKQPADEQPLGIDPEVSSGEASEGACQESDAKVQELEKALEEAQQQAEKYRGEMMRFAADFENFRKQKERELQAAGTRSIENTIRELLPLVDDMKRVMEHAPDDLEQSGEARPYLEGVELLWKNLLKWFERKGVKQIEACGQKLDVNFHEAITQVDHPDAEPDTVIEEYQTGYVMGDKVLRHAKVIVAR

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.097 kDa

MTDPDLHQNDPENPAQASEPVVSKPYIMPDDPETGSAEAYAKEAAEARDKMLRTLAEMENLRKRTAREVADARMYGITGFARDVLDIADNLQRALDAVPAETRANADAGLKSLIEGVELTERSLLNTLEKNGVKKFDPTGQKFDPNFQQAMYEVPDPSVPSGTVVQVVQAGFMIGERVLRPALVGVSKGGAKAAPAASNDQSNSAA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.557 kDa

MSKKASMHKEEKHEKGQHKQPADEQPLGIDPEVSSGEASEGACQESDAKVQELEKALEEAQQQAEKYRGEMMRFAADFENFRKQKERELQAAGTRSIENTIRELLPLVDDMKRVMEHAPDDLEQSGEARPYLEGVELLWKNLLKWFERKGVKQIEACGQKLDVNFHEAITQVDHPDAEPDTVIEEYQTGYVMGDKVLRHAKVIVAR

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.945 kDa

MTDSNGPKDNNQDQAQAAADPVVSKPYIMPDDPEDGANEALIKEAAEARDKMLRTLAEMENLRRRTQKEVADARTYGVSAFARDVLEIADNLQRALDAVPAEARANADAGLKGLIEGVELTERSLINALEKNGVRKFDPSGEKFDPNFQQAMYEVPDPSVPAGTVVQVVQAGFMIGERVLRPALVGVAKGGAKPAPAATNGTDTTA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.969 kDa

MTDSNGQKDNNQDQAQPADPVVSKPYIMPDDPEEGTNEALVREAAEARDKMLRTLAEMENLRRRTAKEVADARTYGVSAFARDVLEIADNLQRALDAVPAEARANADAGLKGLIEGVELTERSLINALEKNGVKKFDPQGEKFDPNFQQAMYEVPDPSVPAGTVVQVVQAGFMIGERVLRPALVGVSKGGAKPAPAAANGNEGGVA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.68 kDa

MSNESIKAEQDLIQEGVESEVSTAEASLIDELTQANFRIEELEQLLAEALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALMGTNPEDEATKSIYQGVELTQKSLLTAVAKFGVKQIDPQGQSFNPDQHQAIGMQPSAEFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPNQESATIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.68 kDa

MSNESIKAEQDLIQEGVESEVSTAEASLIDELTQANFRIEELEQLLAEALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALMGTNPEDEATKSIYQGVELTQKSLLTAVAKFGVKQIDPQGQSFNPDQHQAIGMQPSAEFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPNQESATIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.68 kDa

MSNESIKAEQDLIQEGVESEVSTAEASLIDELTQANFRIEELEQLLAEALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALMGTNPEDEATKSIYQGVELTQKSLLTAVAKFGVKQIDPQGQSFNPDQHQAIGMQPSAEFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPNQESATIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.68 kDa

MSNESIKAEQDLIQEGVESEVSTAEASLIDELTQANFRIEELEQLLAEALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALMGTNPEDEATKSIYQGVELTQKSLLTAVAKFGVKQIDPQGQSFNPDQHQAIGMQPSAEFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPNQESATIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.703 kDa

MSNESIKAEQDLIHEGVESEVSTEEASLIDELTQANFRIEELEQLLADALAKVDEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALQGTNPQDETTKAIYEGVELTQKSLLTAVAKFGVKQIDPQGQAFNPDQHQAIGMQPSAEFPTNTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQESASIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.609 kDa

MSNESIKAEQDLIQEGVESEVSTAEASLVDELTQANFRIEELEQLLADALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALMGTNPEDEATKAIYQGVELTQKSLLTAVAKFGVKQIDPQGESFNPDQHQAIGMQPSADFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQETATIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.68 kDa

MSNESIKAEQDLIQEGVESEVSTEEASLIDELTQANFRIEELEQLLADALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALQGTNPQDETTKALFEGVELTQKSFLTAVAKFGVKPIDPQGQAFNPDQHQAIGMQPSAEYPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQESASINIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.609 kDa

MSNESIKAEQDLIQEGVESEVSTAEASLVDELTQANFRIEELEQLLADALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALMGTNPEDEATKAIYQGVELTQKSLLTAVAKFGVKQIDPQGESFNPDQHQAIGMQPSADFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQETATIDIEA

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.833 kDa

MTEDKKTIPEEQVEAEQVVVEEVEAELVENDESAQPQEEAEASNEDLNMIEVLNKKLALAEQQIVDQQADVARAQADVVNARRIAAQDVQKAHKFALVKFADGLLPVIDSLEMAISHADKEDETLKPMIEGVELTLKSMLDTVDKFGLKVIDPKDEAFDPEKHQAMSMRAVPDVAPNQVIAVMQKGYELNGRVIRPAMVMVSKAED

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.724 kDa

MDKKNEQQEVREENDTSINQESETQVELEEEVVNEECETSSEKTDEKEVDDENVTDINSKLAEKKLQDELDELNDKYQRLQAEYANYRRRTQQEKETIGVFANEKIITELIPVIDSMERALDACEDKEDTMYKGISLVHKQLIDTLVKFGVEEIEAESKEFDPNLHLAVMQESVDGVEANQIVMVLQKGYKLGTKVVRPSMVKVSC

grpE

Protein GrpE

206 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.046 kDa

MNNEDKKLQDEQLQKETVEAAETVSAEEEFVEITAEEMQIARIAELEAALLSSDAKVKEAQDNVLRARAEGENVRRRSEVEIDKARKFALNKFTEELLPVIDNLERAIETADKNDEALKSMIEGVELTLKTMTATVEKFGLKQHNPVGEVFNPEFHQAMSIQESADHEPNTVMLVMQKGYELNGRIIRPAMVMVSKAAAGSVDMQA

grpE

Protein GrpE

205 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.514 kDa

MSKESNKAQEPQIEETEAVAVETEVVEDAASLMDELTQANFRVEELEQALAAAEAKVEEQKDSVIRAAAEVENVRRRAAIDVEKAHKFALEKFANELLPVIDNMERALQGTSSEDEATKAIYEGVELTLKTFTSAVAKFGLTQVDPQGEAFNPDHHQAIGMQPSEEFPANTVMMVMQKGYMLNERLLRPAMVMVSQGGASVDTQA

grpE

Protein GrpE

205 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.09 kDa

MSKEEFPSEKDLPQEDQEKQAKAAEADKAGVKDDKKVKDDKEEAAKPADVELDQLKAEVAALTQKNKDLEDKYLRSQAEIQNAQRRYSKERADLVKYESQRLGKDILSSVDNLERALQVKADDEASRQLKKGIEMTLEGLVRALKDNGIEEIKADGEKFDPTLHQAVQSVPAENDDQKGHVVQVLQKGYVYKDRTLRPAMVVVAQ

grpE

Protein GrpE

205 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.732 kDa

MTDEQTPAEDVAFEADDASQEIEALKLEVAALKDQALRYAAEAENTKRRAERESNDARAYAIQKFARDLLGAADNLSRATAMSPRDSQDPAVTNYIIGVEMTEKELQGAFERNGLKKIDPAKGEKFDPHLHQAVMEQPSTEVAAGGVLQVLQAGYELMGRLVRPAMVAVAAKGSTGPGAPAEPAAAPNPYASNGADTGGSFDTKA

grpE

Protein GrpE

205 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.158 kDa

MSEEVKNSVETEENKASKDNATQAPNPTENHNTAQETEKAENSEKTESATQENESLDKLKKDVTNYREQLLRTVADFENLKKQKEREVASVRKFADESLIKELLPVLDDIERVLVNASKFLQASPEAQSYVDGVKLIQQNMMKVFEARGLKRIEAVGTPFDVHLHEALSQMEKEGAEPDTVIQEFAPGYTLNDKVVRHSKVIVSK

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.411 kDa

MTEDIKEEEVKEEEATETTEEVVEETKEATETTEEVVEGTKEATETTEEVVEETKETSELEEAQARAEEFENKYLRVHAEMQNIQRRAKEERQQLQKYRSQDLAKAILPSLDNIERALAVEGLTDDVKKGLEMIQESLINGLKEEGIEEIAADGEFDHNFHMAIQTMPADDEHPADTIAQVFQKGYKLHDRILRPAMVVVYKEN

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.112 kDa

MSNEEQAQKDDAQPVNEAAIDATAEQADAEVEELSAEQARILELEAALAASEATLAAQKDSVMRAIADADNVRKRAEGEVDKARKFALEKFASELLPVADNLERALQVADKENEAIKPVIEGVDITLKSFVSSIEKFGMKVIDPQGETFNPEQHQAMSMQENAELPANTVMAVMQKGYELNGRLLRPAMVMVSRAPEGGVDTQA

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.985 kDa

MSNQEKKMHEEELQQQETVEADTEAEAEAVGTDADIEWNEESALDETEAKIAQLEAALLSSEAKVKEQQDAVLRAKAEVENMRRRTEQEIDKARKFALNKFAEELLPIIDNLERAIQAADTESEVVQPILEGITLTHKTFIDTISKFGLKEINPEGEAFNPELHQAMSIQESADHESNTVMFVMQKGYELNGRVIRPAMVMVAK

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.112 kDa

MSNEEQAQKDDAQPVNEAAIDATAEQADAEVEELSAEQARILELEAALAASEATLAAQKDSVMRAIADADNVRKRAEGEVDKARKFALEKFASELLPVADNLERALQVADKENEAIKPVIEGVDITLKSFVSSIEKFGMKVIDPQGETFNPEQHQAMSMQENAELPANTVMAVMQKGYELNGRLLRPAMVMVSRAPEGGVDTQA

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.985 kDa

MSNQEKKMHEEELQQQETVEADTEAEAEAVGTDADIEWNEESALDETEAKIAQLEAALLSSEAKVKEQQDAVLRAKAEVENMRRRTEQEIDKARKFALNKFAEELLPIIDNLERAIQAADTESEVVQPILEGITLTHKTFIDTISKFGLKEINPEGEAFNPELHQAMSIQESADHESNTVMFVMQKGYELNGRVIRPAMVMVAK

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.834 kDa

MSSKNNPESETKAKNKWEKVMEAEEEQEEGGGDGSQEMEPHREGLEFPSREKLEGQLTRMEHKVDEYKTQYLRAQAEMDNLRKRIEREKADIIKFGSKQLITDLLPVADSLIHGLESPASEDPQVKSMRDGMSLTLDLLHNTLAKHGVQVINPNPGDPFDPALHEAMSVQAVPDAKPDTIIQVLQKGYQLNGRVLRAARVIVAG

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.952 kDa

MSSKNNPESETKAKNKWEKVMEAEEEQEEGRGDGSQEMEPHREGLEFPSREKLEGQLTRMERKVDEYKTQYLRAQAEMDNLRKRIEREKADIIKFGSKQLITDLLPVADSLIHGLESPASEDPQVKSMRDGMSLTLDLLHNTLAKHGVQVINPNPGDPFDPALHEAMSVQAVPDAKPDTIIQVLQKGYQLNGRVLRAARVIVAG

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.952 kDa

MSSKNNPESETKAKNKWEKVMEAEEEQEEGRGDGSQEMEPHREGLEFPSREKLEGQLTRMERKVDEYKTQYLRAQAEMDNLRKRIEREKADIIKFGSKQLITDLLPVADSLIHGLESPASEDPQVKSMRDGMSLTLDLLHNTLAKHGVQVINPNPGDPFDPALHEAMSVQAVPDAKPDTIIQVLQKGYQLNGRVLRAARVIVAG

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

24.168 kDa

MEELEKDKIERNEEMSEEVKGEGPPSELEQSEEVVEEKIETEVEQKKEPSLEEIVEELRKKLEEKEKEAKEYLDIAQRIKAEFDNYRKRTEKEKAEMISYGQEQVIIELLPVIDNFERALANEGDYNSLREGLELIYRQFKKVLDKFEVREIEAEGQMFDPYKHHALAQEEVEGKQPNEIIEVFQKGYYLKDKVIRPSLVKVAK

grpE

Protein GrpE

204 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.139 kDa

MTDETAKNGPDAAADAQIEPQVQEETNSTAEDAGQDNNPTAALQAENAELRDRFLRLAAEMDNLRRRTERDVKDAKSYAVTAFARDMLAVSDNLRRAIDAVPAEAKEEAQAGLTALIEGVEMTERAMLSTLERHGVRKIEPEGQKFDPNFHQAMFEIPNPQVPNNTVVQVVQPGYTIGDRVLRPAMVGVAKGGPKAETAQAADA

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.181 kDa

MSSKEQNVHEEQVSKEKEGMESVMNESQEQVKSEDAQAEFDAQAELVQALARVDELEKQLQQSQKTEREAMIRAQAEIENIRRRTQQDVEKAHKFALEKFSNELLPVLDNLERALSAADHENEQMQPMIEGLELTLKSFLDAVRKFGIEVVEEKNVAFNPEVHQAMTLIDSPEHEANHVVDVMQKGYTLNGRLLRPAMVVVSK

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.181 kDa

MSSKEQNVHEEQVSKEKEGMESVMNESQEQVKSEDAQAEFDAQAELVQALARVDELEKQLQQSQKTEREAMIRAQAEIENIRRRTQQDVEKAHKFALEKFSNELLPVLDNLERALSAADHENEQMQPMIEGLELTLKSFLDAVRKFGIEVVEEKNVAFNPEVHQAMTLIDSPEHEANHVVDVMQKGYTLNGRLLRPAMVVVSK

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.98 kDa

MTQDQTAEQMPAAESADQSADQGPAAESAAPPAVDSERIKELEAEIAKLKNDVLYAKAETENTRRRLEQQAEDRGRYAISNIAKDVLSVADNLRRALDSVPASAREGNESLTALTTGVEMTERELLATFERYGIKLVAAQGERFDPNLHQAMMEMEDPSQIEGTVVLVMQAGYTLHDRLLRPALVGVAKGGPKSGGNNVDTKV

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.4 kDa

MSNESIKAEQDLIQEGVESEVSTEEASLIDELTQANFRIEELEQLLADALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALQGTNPQDETTKAIYEGVELTQKSLLTAVAKFGVKPIDPQGQAFNPDQHQAIGMQPSAEFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQEINIEA

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.45 kDa

MSNESIKAEQDLIQEGVESEVSTEEASLIDELTQANFRIEELEQLLADALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALQGTNPQDETTKAIYEGVELTQKSFLTAVAKFGVKPIDPQGQAFNPDQHQAIGMQPSAEYPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQEINIEA

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.044 kDa

MSDNGDNNTKSPQHNNPQPNEKSDGKVQPGQPQVNPQRKFTAGINKKKEKLNEDLSELDKLRQQLIHFQNQFRLAVADKENVKRIMQKNIDDTSIYAISNFARDLLSSCDNLETSLKNLKEGDSIHAGVLMTYKELLNTLERHNITRIDPIGEKFNPQFHKAVSQMVDAEKDDNTILHVVQPGYIIKDKLLRAASVIISKKSD

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.496 kDa

MSEQRQNPEQEVELNEDLAKMEADVEAAVQAAEEHAEQEQSPEAEIAMLYAELEVAKQTIADQKDGVVRAAADVENMRRRAAQDVEKAHKFALEKFANELLPVIDNLERAIEFSDKENETLKPVLEGISMTVKSFNDAVAKFGVEIVNPQGEQFNPEFHQAMSIQPSNDVSPNTVLAVMQKGYTLNGRLLRPAMVMVSKAADA

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.731 kDa

MFKGGEKMEKEQRTYDETLEQHEDAQSEQAPEEQVEQVENEATQQEEKDELTVAYEKIAQLEAKLAETENRFLRLHADFDNYRRRVRLDMEAAEKYRAQSLVSDLLPILDNFERALQVQVEDEKAKLLLQGMEMVYRSLIEALKKEGVEAIESVGKPFDPHVHQAVMQVDDQNYEPNTVVEEFQKGYKLKDRVIRPAMVKVNQ

grpE

Protein GrpE

203 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.588 kDa

MTEQNESAFNENEEVNEETSQTDSVENNDETTETSQDNLQEDDSQEIAEDVDPKDEEIQQLKKDVQENEEKYLRLYAEFENYKRRIQKENQTMKAYKAQDVLNDILPTIDNIERALQIDGEDEQFKSLKKGVEMVHESLLNALKNNGLEKIETEGQQFDPNVHQAVVQDDNPDFESGQITQELQSGYKLKERVLRPSMVKVNQ

grpE

Protein GrpE

202 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.507 kDa

MKDKDIKEEVLKEEINKEVNEELKNEEVKEETHEHEHKHGGHTCCGKHGHKHNDEEIGKLKAEIEEWKNEYLRKQADFQNFTKRKEKEVDELKKFASEKIITQFLGSLDNLERAIESSIESKDFDSLLKGIEMIVRNLKDIMSAEGVEEIKTEGVYDPVYHHAVGVEANEDFKEDEIVKVLQKGYMMKGKVIRPAMVIVCKK

grpE

Protein GrpE

202 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.507 kDa

MKDKDIKEEVLKEEINKEVNEELKNEEVKEETHEHEHKHGGHTCCGKHGHKHNDEEIGKLKAEIEEWKNEYLRKQADFQNFTKRKEKEVDELKKFASEKIITQFLGSLDNLERAIESSIESKDFDSLLKGIEMIVRNLKDIMSAEGVEEIKTEGVYDPVYHHAVGVEANEDFKEDEIVKVLQKGYMMKGKVIRPAMVIVCKK

grpE

Protein GrpE

202 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.473 kDa

MENTQENPTSQNPTPADEAARQAAEAASGEPQDQARQPAAAAGEQPAQAQPAGAEAALAEAQAKLAELQESFLRAKAETENVRRRGQEDVAKAHKFAIESFAEHLLPVMDSLEAAVAHSTDDLAKVREGVELTLRQLTGALEKGKVVALNPVGEKFDPHRHQAISMVPADQEPNTVVAVLQKGYVIADRVLRPALVTVAAPK

grpE

Protein GrpE

201 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.655 kDa

MTDRDRQPEDTTAPTGEPVVSKPYIMPDDPEPGSVELLQKEAAEARDRMLRTLAEMENLRKRTTKEVADARLYGITGFARDVLDIADNLQRALDAVPAEARAAADPGLTSLIEGVELTERSLLNALEKHGVKKFDPQGQKFDPNFQQAMFEVPDASVPAGTVVQVMQAGYTIGERVLRPALVGVAKGGAKAASAANSNEVN

grpE

Protein GrpE

201 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.655 kDa

MTDRDRQPEDTTAPTGEPVVSKPYIMPDDPEPGSVELLQKEAAEARDRMLRTLAEMENLRKRTTKEVADARLYGITGFARDVLDIADNLQRALDAVPAEARAAADPGLTSLIEGVELTERSLLNALEKHGVKKFDPQGQKFDPNFQQAMFEVPDASVPAGTVVQVMQAGYTIGERVLRPALVGVAKGGAKAASAANSNEVN

grpE

Protein GrpE

201 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.294 kDa

MSTEPTNQDQAPIDEALTQEVAQDEASLMDELTQANFRVEELEQLLAESQAALAERKDVEMRAAAETQNIRTRAAKDVEQARKFALEKFANELLPVIDNMERALQGTNPEDEATKAIYEGVELTMKGFLTSVEKFGVKQVNPQGETFNPDHHQAIGMQPSPDFPANTVMMVMQKGYLLNDRLLRPAMVMVSQGGPSVDIEA

grpE

Protein GrpE

201 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.249 kDa

MSNESNNTSQDQVEEAVTPEIVVDEASLMDELTQANFRIEELEQLLAESETALAERKDVEMRAAAETQNIRTRAAKDVEQARKFALEKFANELLPVIDNMERALQGTNPEDEATKAIYEGVELTMKGFLTSVEKFGVTQVNPQGQAFNPEHHQAIGMQPSAEYPANTVMMVMQKGYLLNDRLLRPAMVMVSQGGGSVDVEA

grpE

Protein GrpE

201 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.983 kDa

MTDSTNNQGTSGRPDDDHTTEEVASVFNDPGAQAPAGEPDPFVVLENLQLENAGLKDKVLRTYADMENLRRRSEKEVADAKLYGVTSFARDMLTFADNLHRAIESLPAEAKQAVDGPLKTFVEGIELTERDFLSRLAKYGVKKIEPLGNKFDPNLHEALFEIPDESVVSGTVKQVVEDGYVIGERVLRPAKVGVSRGGPKA

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.555 kDa

MTDNDGQKDFSEAAAENAGSKPGEPRVSKPYIMPDDPEETPSEALVKEAAEAKDRMLRTLAEMENLRKRTQREVADARAYGIAGFARDVLEIADNLQRALDAVPAEARAAADPGLTALIEGVELTERSLHRALEKNGVKKLDAAGEKFDPNIHQAMFEVPDNSVPPGTVVQVIQTGYMIGDRVLRPALVGVSKAEPKPAA

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.754 kDa

MEEEIKETSEDKEEENTEAEAVENNEKSEENAGNVEEDEITALKKRIEELENESADMKNKYMYAMAEAENIRKRTAKEKADSIKRANKGLLLSLLTFMDNFERALKAGEQDSNVQGSEYYKGIELIHKQFIDFMHDNGVSEIESLGEEFDPNVHEALTMIEVPDIDKEKVVEVYAKGYKLNDELLRTAKVVVGKPAAAKE

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.997 kDa

MDKKKHGTVQSADETIAAAGFAGEAAQGKGEDVQSVAAEERIRQLETELAAKEAEAAANWDKFVRERADLENYRRRTQKEKEELLKYGNESLLQDILPVVDSMERALGHADSESLSAVIEGIRMTHGMLLGTLKKFGVVAVEAERGTVFDPAYHQAMCQVEVSELPPNTVVEVFQRGYLLNERLLRPAMVSVATVPKDAA

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.659 kDa

MSNEEIKNKDEQLQQDAVETEAEVVGTDADIDWNQAADEIDEKEAKIAQLEAALLVSEERVKEQQDSVLRARAEVENMRRRSEQEVDKARKFALSRFAEELLPVIDNLERAIQAADGEVEAIKPLLEGVELTHKTFVDTIAKFGLKEINPHGEVFNPEFHQAMSIQESAEHEPNTVMFVMQKGYELNGRVLRPAMVMVSK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.659 kDa

MSNEEIKNKDEQLQQDAVETEAEVVGTDADIDWNQAADEIDEKEAKIAQLEAALLVSEERVKEQQDSVLRARAEVENMRRRSEQEVDKARKFALSRFAEELLPVIDNLERAIQAADGEVEAIKPLLEGVELTHKTFVDTIAKFGLKEINPHGEVFNPEFHQAMSIQESAEHEPNTVMFVMQKGYELNGRVLRPAMVMVSK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.659 kDa

MSNEEIKNKDEQLQQDAVETEAEVVGTDADIDWNQAADEIDEKEAKIAQLEAALLVSEERVKEQQDSVLRARAEVENMRRRSEQEVDKARKFALSRFAEELLPVIDNLERAIQAADGEVEAIKPLLEGVELTHKTFVDTIAKFGLKEINPHGEVFNPEFHQAMSIQESAEHEPNTVMFVMQKGYELNGRVLRPAMVMVSK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.754 kDa

MEEEIKETSEDKEEENTEAEAVENNEKSEENAGNVEEDEITALKKRIEELENESADMKNKYMYAMAEAENIRKRTAKEKADSIKRANKGLLLSLLTFMDNFERALKAGEQDSNVQGSEYYKGIELIHKQFIDFMHDNGVSEIESLGEEFDPNVHEALTMIEVPDIDKEKVVEVYAKGYKLNDELLRTAKVVVGKPAAAKE

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.997 kDa

MDKKKHGTVQSADETIAAAGFAGEAAQGKGEDVQSVAAEERIRQLETELAAKEAEAAANWDKFVRERADLENYRRRTQKEKEELLKYGNESLLQDILPVVDSMERALGHADSESLSAVIEGIRMTHGMLLGTLKKFGVVAVEAERGTVFDPAYHQAMCQVEVSELPPNTVVEVFQRGYLLNERLLRPAMVSVATVPKDAA

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.659 kDa

MSNEEIKNKDEQLQQDAVETEAEVVGTDADIDWNQAADEIDEKEAKIAQLEAALLVSEERVKEQQDSVLRARAEVENMRRRSEQEVDKARKFALSRFAEELLPVIDNLERAIQAADGEVEAIKPLLEGVELTHKTFVDTIAKFGLKEINPHGEVFNPEFHQAMSIQESAEHEPNTVMFVMQKGYELNGRVLRPAMVMVSK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.659 kDa

MSNEEIKNKDEQLQQDAVETEAEVVGTDADIDWNQAADEIDEKEAKIAQLEAALLVSEERVKEQQDSVLRARAEVENMRRRSEQEVDKARKFALSRFAEELLPVIDNLERAIQAADGEVEAIKPLLEGVELTHKTFVDTIAKFGLKEINPHGEVFNPEFHQAMSIQESAEHEPNTVMFVMQKGYELNGRVLRPAMVMVSK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.659 kDa

MSNEEIKNKDEQLQQDAVETEAEVVGTDADIDWNQAADEIDEKEAKIAQLEAALLVSEERVKEQQDSVLRARAEVENMRRRSEQEVDKARKFALSRFAEELLPVIDNLERAIQAADGEVEAIKPLLEGVELTHKTFVDTIAKFGLKEINPHGEVFNPEFHQAMSIQESAEHEPNTVMFVMQKGYELNGRVLRPAMVMVSK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.927 kDa

MNEQPNEELQSEDEQFDPQETVSFEGETAANDEAFAEAGEETRDEEMTRLRGEVEEASKRVLQAQAEAENFRKRLRRDTEAQLKFAGMPLVTDILQVRDNLLRAIEAATTAGDGESAAGLVEGVSMVRKQLDDVLAKHAIKEIPAEGELFDPNFHEAISQMPHPEIASGMVAHVATPGFQMHDRVVRPAQVVVSTGDGSA

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.662 kDa

MQEKDSKDVTMEDEETIASQEEIEVEGNSEESSKEEESNNSEISDENLSEENLKLKDENEKLKNELDAAKDRLLRLSAEYENYRNRTAKEKEGIYTDACSDVINEMLPTLDNLERAASTEGSAEDIKKGVEMVVKQFKNSLSKLGIEEIPSEGKFDPNLHNAVMHIEDEGYGENEVVEVLQKGYKRGDKVLRHSMVKVAN

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.412 kDa

MKWRHDYMAEKKVEDLEMDLNEEELEESEVNEDKEFEELDKSEEENEVEELISTLKDENEKLNNEMEALKDRLLRTTGEYDNYRKRTDREKEGLYASACEDVLKEILPVLDNLERAILAKGDIEDLKKGVDMTLKQFKDSFKNLGVEEISTENGFDPNLHDAVMHVEDSQYGEKEVVEVFLKGYKKGDKIIRHSMVKVAN

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.12 kDa

MSNQTNKAQDNQVEEIVEGELLNENGTEATGEASLMDELTQANFRVEELEKALQEAETKVESQKDSVIRAAAEVDNIRRRSAIDVEKAHKFALEKFINELLPVLDNMERALQGTDAEAEATKAIYEGVELTAKSFVSTVEKFGLTQVDPLGDTFNPELHQAIGMQPSADFPANTVMMVMQKGYTLNDRLLRPAMVMVSQG

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.209 kDa

MSNQTNKAQDNQVEEIVEGELLNENATEATDEASLMDELTQANFRVEELEKALQEAEAKVDAQKDSVIRAAAEVDNIRRRSAMDVEKAHKFALEKFINELLPVLDNMERALQGTDAEAEATKAIYEGVELTAKSFMSTVEKFGLVQVDPQGDTFNPELHQAIGMQPSADFPANTVMMVMQKGYTLNERLLRPAMVMVSQG

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.072 kDa

MSNETNKAQDNQIDEQVESIVEGELLTEGSDEASLMDELTQANFRVEELEKALQEAQSTVDSQKDSVIRAAAEVDNIRRRAAIDVEKARKFALEKFANELLPVLDNMERALQGTDAEAEATKAIYEGVELTAKSFVSAVEKFGLTQVDPQGEAFNPELHQAIGMQPSTDFAANTVMMVMQKGYTLNERLLRPAMVMVSQG

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.89 kDa

MSNESTNPQQEPLEQVQDTEVVTDEAALVDELTQANFRIEELEQALAAAEAKVEEQKDSVVRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALAGTNAEDEATKAMYEGVSLTMKTLVNAVEKFGVKVVDPMGQPFNPEQHQAIGMQPNPEVPANHVMVVLQKGYELNGRLLRPAMVMVSQGGGVDTQA

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.066 kDa

MTEELKNKKNNKNYYSQNKNKTKAEFQKPHVKKNQYLKLKTKLDTALLEVQNLKDLNETLKKDIESERQLNLAEISNLTKKYNQKEIEIQKYGASKLARDLIQPLEILKKVVNAPNNNEVVQAYVKGFEMIVSQINNVLESHHIKAMNVKVGDMFNPHLHDANEAVESDEYKTNQIVGVLSDGYMIHDKVLIYAIVKVAK

grpE

Protein GrpE

200 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.086 kDa

MTEELKNKKINKKYYSQNRNKTKAEFQKADIKKNQYLNLKTKLNNVLLEVQNLKELNETLKKELKSEKQLNLAEISNLTKKYNQKELETKKYGASNLAKDLIQPLEILKKVVNAPNNNEVVQAYVKGFEMIINQINNVLESHHIKAMNVKVGDMFDPHLHDANEAVETDEYKTNQIVGVLSDGYMIHDKVLVYAIVKVAK

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.205 kDa

MKDKEIKEEVLKEEINKEVNEKKKCECEEGKEEAHEHKNDEHACCGKHNHKEEIEKLKAEIEEWKNSFLRKQADFQNFTKRKEKEVDELKKFASEKIITQFLGSLDNFERAIESSSESKDFDSLLQGVEMIVRNLKDIMSSEDVEEIPTEGAFNPEYHHAVGVETSEDKKEDEIVKVLQKGYMMKGKVIRPAMVIVCKK

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

23.205 kDa

MKDKEIKEEVLKEEINKEVNEKKKCECEEGKEEAHEHKNDEHACCGKHNHKEEIEKLKAEIEEWKNSFLRKQADFQNFTKRKEKEVDELKKFASEKIITQFLGSLDNFERAIESSSESKDFDSLLQGVEMIVRNLKDIMSSEDVEEIPTEGAFNPEYHHAVGVETSEDKKEDEIVKVLQKGYMMKGKVIRPAMVIVCKK

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.138 kDa

MEKKKHGTNSISEALKVKAAVEQETATPEPTPQSETESADKIKQLEEALAAKEAEAAANWDKVLRERADLENYRKRVQKEKEELLKYGNESLILEILPAIDNMERALEHACDESMSAIVEGIKMTLCMLQSTLKKFGVAPVDAGKGTTFDPAYHQAMNQVESSEHEPNTIVSEFQKGYLLNERLLRPALVSVATAPKEQ

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.154 kDa

MTNQTEKEQVEQDVSQATELAQEAQEAQTQDVEPELQQNNEIDPLEEAIARVQELEAYIAEADKREQDIQLRARAEVENIRRRAEQDVEKAHKFALEKFSKEMLTVVDNLERGLQALEGVDESVKSGVELTHKGLVSTLNNFGVEAVGVVGEAFNPELHQAISMQPAEGIEANHISVVLQKGYTLHGRVIRPAMVMVAS

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.842 kDa

MSDSDNNTKSQQNNPTQTDEKSGEEIQSNQKPQRKFTAVLNKKKEKLNEDLSELDKLKQQLAHFQNQFRLAVADKENVKRIMQKNIDDTSIYAISNFARDLLSSCDNLETSLKNLKEDDSIHAGVLMTYKELLNTLERHNITRIDPIGEKFNPQFHKAVSQMTDEDKDENTILHVVQPGYIIKDKLLRPASVIISKKSD

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.145 kDa

MSEQNTNHESPEQNVAHDNIEHSDSILEETMKEFDPQHNSGEEMTIENEIDLDTFKARIAELEGEVKEAKEGTARANAEAYDAQKRMEQEADKSKKFALQKFARELLEIVDNLERAIENADANDPVAEGVQLTHKALLAVLHKNGIEVVDPQGEKFNADLHEAVDIDAEAEADTVGTVLQKGYSLNGRLLRPAMVRVGQ

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.443 kDa

MAKKSTRTTPEDSQASTTDSAATSTASEATQAATSATDDQAEQTTAVDPTQQITDLKAQLDAKDDQLLRAQAEIVNMQNRNKKEQAALLKYDGQALAKDVLPVLDNLERALATPADDEAAQQLKKGVEMVYGHLQDALKKHGVTEVAAAGEKFDPNIHQAVQTVPVDDDHPADTVVQVLQRGYLLKDRTLRPAMVVVAQ

grpE

Protein GrpE

199 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.218 kDa

MSEQEQKQEQPIENAAENSAQKPEEVTETDVQTEQNVTDPLEEAIARVQELEEQLADAAKKEQDALLRARAEVDNMRRRAEQDVEKAHKFALEKFAKDLLNTIDNLERALATPANVEDESVKGLFDGVELTLKELLATVARFGIEPVGLVGESFNPEFHQAISMQPTEGFETNQITTVLQKGYLLNSRVIRPAMVMVAA

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

21.716 kDa

MVEKKKSQAEKNNQSATEEEIEKAVKGSKRDSNAADEKNSASAAASSSAVSDAEPAVDYEDKFYRAEAEMQNMQQRFNKERASILKYEGQDLAKSILPALDNLERALSVSAGDPASKKIQDGVELTYKSLSNALTDNGIVKIGRAGDQFDPNLHNAIQKTPIDDPEKQKEGTIAVVLQKGYQLHDRVLRPAMVSVYTK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.308 kDa

MSNEENKVTEEELDQIIEEAEKVEAAAQEAEAELEEIGDEKDAKIAQLEAALLSSETKVKDQQDAVLRSKAEVENMRRRTEQEIDKARKYALNKFAEELLPVIDNLERAIQAADAEHEVVKPILEGVELTHKTFVDAVSKFGLKEINPEGEAFNPEFHQAMSIQESPDHESNTVMFVMQKGYELNGRVVRPAMVMVAK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.369 kDa

MSNEENKVTEEELDQIIEEAEKVEAAAQEAEAELEEIGDEKDAKIAQLEAALLSSETKVKDQQDAVLRAKAEVENMRRRTEQEIDKARKYALNKFAEELLPVIDNLERAIQAADTENEVIKPILEGVELTHKTFVDVVAKFGLKEINPEGETFNPEFHQAMSIQESPDHESNTVMFVMQKGYELNGRVIRPAMVMVAK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.305 kDa

MSNEENKINEEALKQQDAAEVEVEAVGTDADIEWNEEADESAVKIAELEAALLASEARVKEQQDSVLRAKAEVENMRRRTEQEIDKARKYALNRFAEELLPVIDNLERAIQAADAESEAVKPLLEGVELTHKTFVDVVSKFGLKEINPEGQPFNPEWHQAMSIQESPDHESNTVMFVMQKGYELNGRVIRPAMVMVAK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.308 kDa

MSNEENKVTEEELDQIIEEAEKVEAAAQEAEAELEEIGDEKDAKIAQLEAALLSSETKVKDQQDAVLRSKAEVENMRRRTEQEIDKARKYALNKFAEELLPVIDNLERAIQAADAEHEVVKPILEGVELTHKTFVDAVSKFGLKEINPEGEAFNPEFHQAMSIQESPDHESNTVMFVMQKGYELNGRVVRPAMVMVAK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.369 kDa

MSNEENKVTEEELDQIIEEAEKVEAAAQEAEAELEEIGDEKDAKIAQLEAALLSSETKVKDQQDAVLRAKAEVENMRRRTEQEIDKARKYALNKFAEELLPVIDNLERAIQAADTENEVIKPILEGVELTHKTFVDVVAKFGLKEINPEGETFNPEFHQAMSIQESPDHESNTVMFVMQKGYELNGRVIRPAMVMVAK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.305 kDa

MSNEENKINEEALKQQDAAEVEVEAVGTDADIEWNEEADESAVKIAELEAALLASEARVKEQQDSVLRAKAEVENMRRRTEQEIDKARKYALNRFAEELLPVIDNLERAIQAADAESEAVKPLLEGVELTHKTFVDVVSKFGLKEINPEGQPFNPEWHQAMSIQESPDHESNTVMFVMQKGYELNGRVIRPAMVMVAK

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.046 kDa

MTTEKETATPADVEVASQEEQIDQTTEAQVEEPSIEAELAGCYAKIHELETYIAEADKREQDIQLRAQAEIQNIRRRTEQDIEKAHKFALEKFAKELLTVVDNLERGLVALDTAVTDEKTQALVDGVEMTHKEFVSTLAKFGIEAIGEIGDVFNPELHQAISMQPAENIEANHLSQVLQKGYTLQGRVIRPAMVMVAA

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.298 kDa

MSEQEQKVEIPEVEKQEEVVVEETQQAEHSQEFDPLEEAIARVQELEEQLKTQIEEAANKEQDILLRSRAEIENLRRRTEQDVEKAHKFALEKFSKDILNTIDNLERALATPANKEDESVKALFDGVELTLKELVSTVGRFGVEAVGVVGEAFNPDLHQAISMQPAEGFETNQISVVLQKGYTLNGRVIRPAMVMVAA

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.

22.813 kDa

MIMRRIQVTETTENKDLVQGDVQAETATEEVERSEVQEEIELSVEEQYEANVAELQAKLDDDEENRHLRLRADFDNMRRRQQLDGEAAEKYRAQSLLSDLLPVLDNFERALQVETTSEETASIIKGIEMVYRSLLEATVFEGLQVIKAEGEQFDPNIHQAVMQEQDSEKETGVVLRELQKGYILKDRVLRPTMVSVNE

grpE

Protein GrpE

198 amino acids

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Belongs to the GrpE family.