ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family.

Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.

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

Chaperone protein htpG; Molecular chaperone. Has ATPase activity.

Hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Hypothetical protein.

Co-chaperone HSP-70 protein; 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 [...]

Transcriptional regulator belonging to the LysR family. Features a N-terminal helix-turn-helix DNA binding domain and a C-terminal LysR-like substrate binding domain. Localized in the cytoplasm; Specificity unclear.