Co-chaperone GrpE; 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-depend [...]

Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.

Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.

Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Identified by match to protein family HMM PF00012.

Putative DnaJ domain protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556.

Putative ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.