Rv2232, (MTCY427.13), len: 291 aa. PtkA, protein tyrosine kinase, similar to members of haloacid dehalogenase-like family from several bacteria and to putative phosphatases e.g. Q9I767 and AAK78398. Contains N-terminal extension. FASTA scores: Q9I767 hypothetical protein PA0065 (221 aa) opt: 439 E(): 3.2e-18; 38.679% identity (40.196% ungapped) in 212 aa overlap; >>tr|AAK78398 Predicted phosphatase, had family (216 aa) opt: 427, E(): 1.5e-17; 34.762% identity (35.437% ungapped) in 210 aa overlap. Replaces previous Rv2232 and Rv2233. Predicted to be an outer membrane protein (See Song e [...]

Rv2235, (MTCY427.16), len: 271 aa. Probable conserved transmembrane protein (see Miller & Shinnick 2001); hydrophobic regions near N- and C-terminus. Similar to conserved membrane proteins in other Actinomycetes. Equivalent to Mycobacterium leprae. ML1644 (270 aa). FASTA scores: opt: 1357, E(): 1.2e-72; 74.170% identity in 271 aa overlap T44717|3150235|CAA19213.1|AL023635 13093419|CAC30595.1|AL583922. A core mycobacterial gene; conserved in mycobacterial strains (See Marmiesse et al.,2004).

Acid phosphatase (acid phosphomonoesterase) (phosphomonoesterase) (glycerophosphatase); Virulence factor that plays an important role in blocking phagosome-lysosome fusion and thus participates in the intracellular survival of the pathogen. Acts as a phosphatase that dephosphorylates phosphatidylinositol 3-phosphate (PI3P), a membrane trafficking regulatory lipid essential for phagosomal acquisition of lysosomal constituents. Therefore, SapM eliminates PI3P from the phagosomal membrane by catalyzing its hydrolysis, and thus contributes to inhibition of phagosome maturation. Also interf [...]

Multifunctional protein. Has RNASE H,alpha-ribazole phosphatase, and acid phosphatase activities; Endonuclease that displays both RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. As the only authenticated RNase HI in M.tuberculosis, probably plays an important role in the physiology of this organism, being likely involved in bacterial replication.

Conserved protein; Rv2230c, (MTCY427.11c), len: 379 aa. Conserved protein. Equivalent to Mycobacterium leprae, ML1639,conserved hypothetical protein (385 aa). Similar to hypothetical proteins from B. subtilis, P54472, and L. monocytogenes, P53434. FASTA score: ML1639 (MLCB1243.36) opt: 2088, E(): 4e-107; 79.481% identity in 385 aa overlap same as >pir||T44719 hypothetical protein MLCB1243.36 [imported] - Mycobacterium leprae >gi|3150237|emb|CAA19217.1| (AL023635); P54472|YQFO_BACSU hypothetical 30. 7 kDa protein in (279 aa) opt: 604; E(): 2.2e-30; 38.8% identity in 258 aa overlap. P534 [...]

Conserved protein; Rv2229c, (MTCY427.10c), len: 245 aa. Conserved protein; probable coiled-coil protein similar to conserved hypothetical proteins in Actinomycetes. Equivalent to Mycobacterium leprae ML1638 (232 aa), FASTA scores: opt: 868 E(): 4.4e-43; 60.870% identity in 230 aa overlap emb|CAC30589.1| (AL583922). A core mycobacterial gene; conserved in mycobacterial strains (See Marmiesse et al.,2004).

Rv2231c, (MTCY427.12c), len: 364 aa. Possible cobC,aminotransferase. Note that initiation codon uncertain. Similar to CobC aminotransferases e.g. sp|P21633|COBC_PSEDE COBC protein (333 aa) opt: 277, E(): 1.7e-11; 28.8% identity in 313 aa overlap and also to e.g. SW:HIS8_ECOLI P06986 histidinol-phosphate aminotransferase (27.0% identity in 289 aa overlap), contains PS00105 aminotransferases class-I pyridoxal-phosphate attachment site. Real Mycobacterium tuberculosis histidinol-phosphate aminotransferase, hisC, is Rv1600 (MTCY336.04c); Belongs to the class-I pyridoxal-phosphate-dependent [...]

Probable nucleoside diphosphate kinase NdkA (NDK) (NDP kinase) (nucleoside-2-P kinase); Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.

Phosphoserine/threonine phosphatase PstP; The only predicted protein phosphatase in M.tuberculosis, it dephosphorylates at least 5 protein kinases (PknA, PknB, PknD, PknE and PknF) and the penicillin-binding protein PBPA.