May play a role in the maturation of mycofactocin, a conserved polypeptide that might serve as an electron carrier. The genes for mycofactocin and other proteins proposed to function in its maturation are found in a conserved gene cluster..

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:8828210}..

May be a desaturase involved in mycobacterial fatty acid biosynthesis. {ECO:0000305|PubMed:14559907}..

Could possibly oxidize fatty acids using specific components. {ECO:0000250}..

Unknown.

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 between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity). Inhibits the beta-lactamase and RNase activity of RNase J. {ECO:0000255|HAMAP-Rule:MF_01152, ECO:0000269|PubMed:21568871}..

Unknown.

Unknown.

Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. Although it has succinate semialdehyde dehydrogenase activity, is likely to act physiologically on a different aldehyde(s). NAD(+) can substitute for NADP(+), but enzymatic activity is three times reduced. {ECO:0000269|PubMed:16027371}..

Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types. {ECO:0000269|PubMed:14671303, ECO:0000269|PubMed:17082771, ECO:0000269|PubMed:19448618, ECO:0000269|PubMed:20355727}..

Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes. {ECO:0000250|UniProtKB:P12425}..

The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). {ECO:0000250}..

An ATPase (PubMed:26396239). Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10) (PubMed:16368961). {ECO:0000269|PubMed:16368961, ECO:0000269|PubMed:26396239}..

Unknown.

Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity). {ECO:0000250}..

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). {ECO:0000250}..

Unknown.

Unknown.

Peptidoglycan polymerase that is essential for cell division. {ECO:0000250|UniProtKB:P39604}..

Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. {ECO:0000255|HAMAP-Rule:MF_00802}..

Plays an important role in mycobacterial pathogenesis in the context of innate immunity. Aids host cell invasion and intracellular bacillary persistence. Increases host oxidative stress response, leading to genomic instability and decrease in macrophage viability. Also induces autophagy and modulates the immune function of macrophages. {ECO:0000269|PubMed:26786654}..

Unknown.

Unknown.

Catalyzes the meta-cleavage of 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (3,4-DHSA) to produce 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid (4,9-DSHA). {ECO:0000269|PubMed:17264217}..

Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan..

Catalyzes the NAD-dependent oxidation of beta-hydroxybutyryl-CoA to acetoacetyl-CoA in vitro at pH 10. Also catalyzes the reverse reaction albeit in a lower pH range of 5.5-6.5. The reverse reaction is able to use NADPH as well as NADH. {ECO:0000269|PubMed:20378648}..

Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. {ECO:0000250|UniProtKB:P33371}..

Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00708}..

GTPase that plays an essential role in the late steps of ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}..

Probably plays a role in host phagosome maturation arrest (PubMed:20844580). {ECO:0000305|PubMed:20844580}..

Catalyzes the F420H(2)-dependent reduction of biliverdin-IXalpha at C10 position, leading to bilirubin-IXalpha, a potent antioxidant. As biliverdin-IXalpha is produced in high amounts in macrophages infected with M.tuberculosis, its reduction by Rv2074 may play a role in protecting mycobacteria against oxidative stress, aiding the persistence of M.tuberculosis infection. {ECO:0000269|PubMed:27364382}..

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000269|PubMed:12515554}..

Unknown.

Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. {ECO:0000269|PubMed:15937179}..

Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine, a step in the biosynthesis pathway of ergothioneine. {ECO:0000250|UniProtKB:A0R5M8}..

Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan..

Unknown.

Unknown.

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}..

Unknown.

DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity). {ECO:0000250}..

Represses transcription of the catalase-peroxidase gene katG and its own transcription by binding to the promoter region in a redox-dependent manner. {ECO:0000269|PubMed:11401695, ECO:0000269|PubMed:12949087}..

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. {ECO:0000250}..

Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}..

Part of the ABC transporter complex Rv2686c/Rv2687c/Rv2688c involved in fluoroquinolones export. Confers resistance to ciprofloxacin and, to a lesser extent, norfloxacin, moxifloxacin and sparfloxacin. Probably responsible for energy coupling to the transport system. {ECO:0000269|PubMed:15273144}..

Unknown.

Unknown.

A secreted protein that plays a number of roles in modulating the host's immune response to infection as well as being responsible for bacterial escape into the host cytoplasm. Acts as a strong host (human) T-cell antigen (PubMed:7729876, PubMed:11940590). Inhibits IL-12 p40 (IL12B) and TNF-alpha expression by infected host (mouse) macrophages, reduces the nitric oxide response by about 75% (PubMed:14557536). In mice previously exposed to the bacterium, elicits high level of IFN-gamma production by T-cells upon subsequent challenge by M.tuberculosis, in the first phase of a protective immune response (PubMed:7897219, PubMed:7729876). Higher levels (1.6-3.3 uM) of recombinant protein inhibit IFN-gamma production by host (human) T-cells and also IL-17 and TNF-alpha production but not IL-2; decreases expression of host ATF-2 and JUN transcription factors by affecting T-cell receptors signaling downstream of ZAP70, without cytotoxicity or apoptosis (PubMed:19265145). EsxA inhibits IFN-gamma production in human T-cells by activating p38 MAPK (MAPK14), p38 MAPK is not responsible for IL-17 decrease (PubMed:21586573). Binds host (mouse) Toll-like receptor 2 (TLR2) and decreases host MYD88-dependent signaling; binding to TLR2 activates host kinase AKT and subsequently inhibits downstream activation of NF-kappa-B; the C-terminal 20 residues (76-95) are necessary and sufficient for the TLR2 inhibitory effect (PubMed:17486091). Required for induction of host (human) IL-1B maturation and release by activating the host NLRP3/ASC inflammasome; may also promote access of other tuberculosis proteins to the host cells cytoplasm (PubMed:20148899). Induces IL-8 (CXCL8) expression in host (human) lung epithelial cells (PubMed:23867456). Exogenously applied protein, or protein expressed in host (human and mouse), binds beta-2-microglobulin (B2M) and decreases its export to the cell surface, probably leading to defects in class I antigen presentation by the host cell (PubMed:25356553). Responsible for mitochondrial fragmention, redistribution around the cell nucleus and decreased mitochondrial mass; this effect is not seen until 48 hours post-infection (PubMed:26092385). Able to disrupt artificial planar bilayers in the absence of EsxB (CFP-10) (PubMed:14557547). Native protein binds artificial liposomes in the absence but not presence of EsxB and is able to rigidify and lyse them; the EsxA-EsxB complex dissociates at acidic pH, EsxB might serve as a chaperone to prevent membrane lysis (PubMed:17557817). Recombinant protein induces leakage of phosphocholine liposomes at acidic pH in the absence of ExsB, undergoes conformational change, becoming more alpha-helical at acidic pH (PubMed:23150662, PubMed:25645924). The study using recombinant protein did not find dissociation of EsxA-EsxB complex at acidic pH (PubMed:23150662). Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm (PubMed:17604718, PubMed:22319448). Translocation into host cytoplasm is visible 3 days post-infection using cultured human cells and precedes host cell death (PubMed:22319448). Recombinant protein induces apoptosis in host (human) differentiated cell lines, which is cell-line dependent; bacteria missing the ESX-1 locus do not induce apoptosis (PubMed:17298391). Host (human) cells treated with EsxA become permeable to extracellular dye (PubMed:17298391). EsxA and EsxA-EsxB are cytotoxic to pneumocytes (PubMed:19906174). ESX-1 secretion system-induced host (mouse) cell apoptosis, which is probably responsible for infection of new host cells, might be due to EsxA (PubMed:23848406). EsxA induces necrosis in aged neutrophils (PubMed:25321481). May help regulate assembly and function of the type VII secretion system (T7SS) (By similarity). EsxA disassembles pre-formed EccC-EsxB multimers, possibly by making EccC-EsxA-EsxB trimers instead of EccC-EsxB-EsxB-EccC tetramers (By similarity). {ECO:0000250|UniProtKB:D1A4H1, ECO:0000269|PubMed:11940590, ECO:0000269|PubMed:14557536, ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:17298391, ECO:0000269|PubMed:17486091, ECO:0000269|PubMed:17557817, ECO:0000269|PubMed:17604718, ECO:0000269|PubMed:19265145, ECO:0000269|PubMed:19906174, ECO:0000269|PubMed:20148899, ECO:0000269|PubMed:21586573, ECO:0000269|PubMed:22319448, ECO:0000269|PubMed:23867456, ECO:0000269|PubMed:25321481, ECO:0000269|PubMed:25356553, ECO:0000269|PubMed:26092385, ECO:0000269|PubMed:26260636, ECO:0000269|PubMed:7729876, ECO:0000269|PubMed:7897219, ECO:0000305|PubMed:23848406}.; FUNCTION: May be critical in pro-bacteria versus pro-host interactions; ESX-1 mediates DNA mediated export (maybe via EsxA). The DNA interacts with host (human) cGAS, leading to cGAMP production and activation of the host STING-TBK-1-IRF-3 signaling pathway that leads to IFN-beta which is thought to be "pro-bacteria". Mycobacterial dsDNA also interacts with AIM2-NLRP3-ASC to activate an inflammasome, leading to the "pro-host" IL-1-beta (PubMed:26048138, PubMed:26048136). {ECO:0000269|PubMed:26048136, ECO:0000269|PubMed:26048138}..

Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10). {ECO:0000269|PubMed:14557536, ECO:0000269|PubMed:16368961, ECO:0000305|PubMed:14557547}..

Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan..