Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); 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 (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family.

Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008).

Rv3446c, (MTCY77.18c), len: 404 aa. Hypothetical unknown ala-, val-rich protein.

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.

Probable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family.

Probable GrpE protein (HSP-70 cofactor); 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. Severa [...]

Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); 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 (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family.

Possible exported alanine and valine rich protein; Rv2668, (MTCY441.37), len: 173 aa. Hypothetical ala-, val-rich protein, possibly exported. Equivalent to AAK47057 from Mycobacterium tuberculosis strain CDC1551 (208 aa) but N-terminal part shorter 35 aa and with few differences. Has potential signal peptide sequence. Predicted to be an outer membrane protein (See Song et al.,2008).

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 [...]