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.

Rv1332, (MTCY130.17), len: 218 aa. Possible regulatory protein, high similarity to ML014|U00014 M. leprae B1549_C3_236 (222 aa), FASTA scores: opt: 1158, E(): 0, (75.6% identity in 221 aa overlap). Helix turn helix motif fram aa 8-29 (+3.03 SD); To M.leprae ML1166.

Rv2667, (MTCY441.36), len: 252 aa. Possible clpC2,ATP-dependent protease atp-binding subunit, highly similar to Q9X8L2|SCE9.40 hypothetical 27.3 KDA protein from Streptomyces coelicolor (258 aa), FASTA scores: opt: 877,E(): 2.2e-46, (57.25% identity in 255 aa overlap). The second half of the protein is highly similar to N-terminal of several CLP-family proteins e.g. P24428|CLPC_MYCLE|ML0235 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium leprae (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); O06286|CLPC_MYCTU|Rv3596c|MT3703 [...]

Probable hydrolase; Aminopeptidase; Belongs to the peptidase S58 family.

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 [...]

Possible hydrolase; Protease that hydrolyzes the covalent CysO-cysteine adduct synthesized by CysM to release L-cysteine and regenerate CysO.

Rv1337, (MTCY130.22), len: 240 aa. Probable integral membrane protein. Highly similar to P53426 hypothetical protein B1549_C3_240 from M.leprae (251); and P74553|D90916 hypothetical protein from Synechocystis sp. (198 aa), FASTA scores: E(): 2.3e-25, (43.6% identity in 181 aa overlap).

Sulfur carrier protein CysO; In its thiocarboxylated form (CysO-COSH), is the sulfur donor in the CysM-dependent cysteine biosynthetic pathway. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the sulfur carrier protein CysO family.

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]