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Search term: Rv2234

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nameptpA
Rv numberRv2234
Synonym(s)MPtpA
TypeCDS
FunctionInvolved in signal transduction (via dephosphorylation). Can dephosphorylated in vitro the phosphotyrosine residue of myelin basic protein (MBP) at pH 7.0 [catalytic activity: protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate].
ProductPhosphotyrosine protein phosphatase PtpA (protein-tyrosine-phosphatase) (PTPase) (LMW phosphatase)
CommentsRv2234, (MTCY427.15), len: 163 aa. PtpA (alternate gene name: MPtpA), low molecular weight protein-tyrosine-phosphatase (see citations below), similar to other phosphotyrosine protein phosphatases e.g. P53433|PTPA_STRCO low molecular weight protein-tyrosine phosphatase from Streptomyces coelicolor (164 aa), FASTA scores: opt: 455, E(): 3.3e -25, (49.7% identity in 155 aa overlap); PA1S_HUMAN|P24667 red cell acid phosphatase 1, FASTA score: (37.7% identity in 138 aa overlap); etc. Contains a phosphatase catalytic site domain located in N-terminal part. Activity proven biochemically. Supposed a secreted protein. Substrate of PtkA|Rv2232.
Molecular mass (Da)17860
Isoelectric point6.5051
Gene length (bp)492
Protein length163
Location (kb)2507.15


Functional categoryregulatory proteins


ProteomicsIdentified in the cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Translational start site supported by proteomics data (See Kelkar et al., 2011).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Growth of M. tuberculosis Erdman ptpA|Rv2234 mutant is comparable to wild-type in vitro and in C57BL/6 mice (See Grundner et al., 2008).
see TB knockouts/mutants availability


Coordinates
TypeStartEndOrientation
RBS25071352507139+
CDS25071462507637+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2234|ptpA
VSDPLHVTFVCTGNICRSPMAEKMFAQQLRHRGLGDAVRVTSAGTGNWHVGSCADERAAG
VLRAHGYPTDHRAAQVGTEHLAADLLVALDRNHARLLRQLGVEAARVRMLRSFDPRSGTH
ALDVEDPYYGDHSDFEEVFAVIESALPGLHDWVDERLARNGPS
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP65716
Protein Data Bank1U2P 1U2Q 1ZOJ


Orthologs/Cross-references
CDC1551MT2293
Enzyme Classification3.1.3.48
Gene Ontologyprotein tyrosine phosphatase activity
protein amino acid dephosphorylation
M. bovisMb2258
M. lepraeML1643
M. marinumMMAR_3309
M. smegmatisMSMEG_4309
UniProtP65716
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2234


Expression Data
TBDBRv2234


Bibliography
Koul A, Choidas A, Treder M, Tyagi AK, Drlica K, Singh Y, Ullrich A,
Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis
J Bacteriol (2000) 182(19):5425-32
Cited for: Product/Biochemistry/Function
Cowley SC, Babakaiff R, Av-Gay Y,
Expression and localization of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA
Res Microbiol (2002) 153(4):233-41
Cited for: Biochemistry/Regulation
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Madhurantakam C, Rajakumara E, Mazumdar PA, Saha B, Mitra D, Wiker HG, Sankaranarayanan R, Das AK,
Crystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution.
J Bacteriol (2005) 187(6):2175-81
Cited for: Structure
Castandet J, Prost JF, Peyron P, Astarie-Dequeker C, Anes E, Cozzone AJ, Griffiths G, Maridonneau-Parini I,
Tyrosine phosphatase MptpA of Mycobacterium tuberculosis inhibits phagocytosis and increases actin polymerization in macrophages.
Res Microbiol (2005) 156(10):1005-13
Cited for: Function
Grundner C, Cox JS, Alber T,
Protein tyrosine phosphatase PtpA is not required for Mycobacterium tuberculosis growth in mice.
FEMS Microbiol Lett (2008) 287(2):181-4
Cited for: Mutant
Bach H, Wong D, Av-Gay Y,
Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA.
Biochem J (2009) 420(2):155-60
Cited for: Biochemistry
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence