Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chaperone protein DnaJ |
Protein Synonyms/Alias | |
Gene Name | dnaJ |
Gene Synonyms/Alias | SYNPCC7002_A0693 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | 231 | TIPAGVDSGTRLRVS | S | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity) |
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| Chaperone; Completeproteome; Cytoplasm; DNAreplication; Metal-binding; Repeat; Stressresponse; Zinc; Zinc-finger |
Protein Sequence | MAGDFYEILG VSRDCGKDEL KRAYRRLARQ YHPDVNKDPG AEEKFKEINR AYEVLSEPET 60 RARYDRFGEA GVSGAGAAGA DYGDMGGFAD IFETIFSGFG GMGTGATGGG RRRSGPMRGD 120 DLRLDLKLDF KEAIFGGEKE IRIPHLETCK TCSGSGAKAG TSANTCGTCN GTGQVRRATR 180 TPFGSFAQVS VCPTCNGEGQ VIAEKCESCG GAGRKQETKK LKITIPAGVD SGTRLRVSRE 240 GDAGVKGGPP GDLYVYLAVN ADKEFRRDGT NILSEIEISY LQAILGDTVK VKTVDGTEDL 300 TIPAGLQPNK VLILEGKGVP KLGNPVSRGD HLITVKVMIP TKVSREEKEL LHQLAKLKGT 360 EHSKGGFEGL LGNLFHNK 378 |
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