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.

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.

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 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 [...]

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.

Rv1691, MTCI125.13, len: 250 aa. Conserved hypothetical protein, similar to Q9S210|SCI51.30C|AL109848 Hypothetical protein from Streptomyces coelicolor (210 aa),FASTA score: opt: 556, E(): 6.4e-27, (50.6% identity in 180 aa overlap).

Conserved hypothetical protein; Required for the sulfation of S881. S881 is a sulfated menaquinone, which is localized in the outer envelope of M.tuberculosis and negatively regulates its virulence. 3'-phosphoadenosine-5'- phosphosulfate (PAPS) is the sulfate donor. Belongs to the Stf3 family.