Probable chaperone protein DnaJ1; 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 [...]

Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...]

Rv0353, (MTCY13E10.13), len: 126 aa. Probable hspR,heat shock regulatory protein (see Stewart et al., 2001),merR family, highly similar to others e.g. HspR|P40183 heat shock regulatory protein from Streptomyces coelicolor (151 aa), FASTA scores: E(): 4.9e-22, (55.7% identity in 140 aa overlap), that binds to three inverted repeats (IR1-IR3) in the promoter region of the dnaK operon. Has possible coiled coil region in C-terminal half. Belongs to the MerR family of transcriptional regulators.

60 kDa chaperonin 2; Prevents aggregation of substrate proteins and promotes their refolding.

10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family.

60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1); Prevents aggregation of substrate proteins and promotes their refolding. Functions in the absence of co-chaperone CH10 and ATP.

Probable chaperone protein DnaJ2; 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 [...]

Probable heat shock protein transcriptional repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons; Belongs to the HrcA family.

Rv0312, (MTCY63.17), len: 620 aa. Conserved hypothetical protein with highly Pro-, Thr-rich C-terminus. Similar to Pro-,Thr-rich region in Rv2264c|AL021925|MTV022_14 from Mycobacterium tuberculosis (592 aa), FASTA scores: opt: 1075, E(): 0, (38.9% identity in 627 aa overlap). Also some similarity with Rv0350|dnaK from Mycobacterium tuberculosis. Possibly membrane protein; has hydrophobic stetch in its middle part.