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

Co-factor of molecular chaperone; 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 betwe [...]

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

Transcriptional regulator of heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity.

Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily.

ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]