Rv2963, (MTCY349.24c), len: 406 aa. Probable integral membrane protein.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

Rv0849, (MTV043.42), len: 419 aa. Probable conserved integral membrane transport protein, possibly member of major facilitator superfamily (MFS) involved in transport of drug, showing similarity with others e.g. T35055 probable transport system permease protein from Streptomyces coelicolor (436 aa); NP_295031.1|NC_001263 major facilitator family protein from Deinococcus radiodurans (458 aa); NP_455659.1|NC_003198 putative membrane transporter from Salmonella enterica subsp. enterica serovar Typhi (402 aa); etc.

Ferrochelatase HemZ (protoheme ferro-lyase) (heme synthetase); Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme.

Rv0850, (MTV043.43), len: 110 aa. Putative transposase (fragment), similar in part to others e.g. Q45144|Q4514 transposable element IS31831 (436 aa), FASTA scores: opt: 175, E(): 4.3e-05, (38.6% identity in 57 aa overlap); etc.

Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily.

Conserved protein; Under low copper conditions, represses the expression of lpqS, Rv2963, mymT, socA, socB, mmcO and its own expression. In the presence of copper, RicR dissociates from DNA, leading to the expression of the target genes. Members of the RicR regulon are important for copper resistance during infections and full virulence in a mouse model of infection.

Metallothionein, MymT; Metallothioneins are small proteins that have a high content of cysteine residues wich allow them to bind heavy metal ions through clusters of thiolate bonds. MymT binds up to seven ions of Cu(+), with a preference for four to six Cu(+) ions, in a solvent-shielded core. MymT protects M.tuberculosis from copper toxicity.