Accession | GenProp0244 |
Name | chaperone system: DnaK-DnaJ-GrpE |
Type | SYSTEM |
Description | DnaK, DnaJ, and GrpE form a chaperone system. DnaK has ATPase activity. DnaJ and GrpE are co-chaperones for DnaK, that is, stimulate this activity. This system is also called the hsp70 heat-shock system. Excluded from this system are the heat shock cognate (Hsc) homologs, which are associated specifically with iron-sulfur cluster biosynthesis (see GenProp0138, the iron-sulfur cluster assembly iscSUA-hscBA-fdx system). The heat shock repressor HrcA is found in about half of bacterial genomes with the DnaK-DnaJ-GrpE heat shock system, usually encoded upstream in a heat shock operon; it is included here as an optional component. |
JCVI Role | Protein folding and stabilization |
Parent Property | GenProp0248: protein folding
|
Literature References | [ 1 ]Brehmer D, Gassler C, Rist W, Mayer MP, Bukau B Influence of GrpE on DnaK-substrate interactions. J Biol Chem 2004 Jul 2;279(27):27957-64. Epub 2004 Apr 21. PMID 15102842 |
|
Web References | The Ecocyc Database: Protein: DnaJ/DnaK/GrpE |
Gene Ontology Term | GO:0006457: protein folding (biological_process) GO:0016481: negative regulation of transcription (biological_process)
|