PTPB_MYCTU
ID PTPB_MYCTU Reviewed; 276 AA.
AC I6WXK4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Triple specificity protein phosphatase PtpB {ECO:0000305};
DE EC=3.1.3.- {ECO:0000269|PubMed:17584180};
DE EC=3.1.3.16 {ECO:0000269|PubMed:17584180};
DE EC=3.1.3.48 {ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:16271885, ECO:0000269|PubMed:17584180};
DE AltName: Full=MPtpB {ECO:0000303|PubMed:10986245};
DE AltName: Full=Phosphoinositide phosphatase {ECO:0000303|PubMed:17584180};
DE AltName: Full=Protein-serine/threonine phosphatase {ECO:0000305};
DE AltName: Full=Protein-tyrosine phosphatase B {ECO:0000305};
DE AltName: Full=TSP PTP {ECO:0000303|PubMed:22136336};
GN Name=ptpB {ECO:0000303|PubMed:16271885};
GN Synonyms=mptpB {ECO:0000303|PubMed:10986245};
GN OrderedLocusNames=Rv0153c {ECO:0000312|EMBL:CCP42878.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF CYS-160.
RC STRAIN=H37Rv;
RX PubMed=10986245; DOI=10.1128/jb.182.19.5425-5432.2000;
RA Koul A., Choidas A., Treder M., Tyagi A.K., Drlica K., Singh Y.,
RA Ullrich A.;
RT "Cloning and characterization of secretory tyrosine phosphatases of
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 182:5425-5432(2000).
RN [3]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RX PubMed=14617138; DOI=10.1046/j.1365-2958.2003.03712.x;
RA Singh R., Rao V., Shakila H., Gupta R., Khera A., Dhar N., Singh A.,
RA Koul A., Singh Y., Naseema M., Narayanan P.R., Paramasivan C.N.,
RA Ramanathan V.D., Tyagi A.K.;
RT "Disruption of mptpB impairs the ability of Mycobacterium tuberculosis to
RT survive in guinea pigs.";
RL Mol. Microbiol. 50:751-762(2003).
RN [4]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RX PubMed=16256440; DOI=10.1016/j.tube.2005.08.015;
RA Singh R., Singh A., Tyagi A.K.;
RT "Deciphering the genes involved in pathogenesis of Mycobacterium
RT tuberculosis.";
RL Tuberculosis 85:325-335(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP AND MUTAGENESIS OF ASP-82; CYS-160; LYS-164; ASP-165 AND ARG-166.
RX PubMed=17584180; DOI=10.1042/bj20070670;
RA Beresford N., Patel S., Armstrong J., Szoeor B., Fordham-Skelton A.P.,
RA Tabernero L.;
RT "MptpB, a virulence factor from Mycobacterium tuberculosis, exhibits
RT triple-specificity phosphatase activity.";
RL Biochem. J. 406:13-18(2007).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=17636914; DOI=10.1021/ja0727520;
RA Soellner M.B., Rawls K.A., Grundner C., Alber T., Ellman J.A.;
RT "Fragment-based substrate activity screening method for the identification
RT of potent inhibitors of the Mycobacterium tuberculosis phosphatase PtpB.";
RL J. Am. Chem. Soc. 129:9613-9615(2007).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=17685373; DOI=10.1002/asia.200700125;
RA Correa I.R. Jr., Noeren-Mueller A., Ambrosi H.D., Jakupovic S., Saxena K.,
RA Schwalbe H., Kaiser M., Waldmann H.;
RT "Identification of inhibitors for mycobacterial protein tyrosine
RT phosphatase B (MptpB) by biology-oriented synthesis (BIOS).";
RL Chem. Asian J. 2:1109-1126(2007).
RN [8]
RP ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RC STRAIN=H37Rv;
RX PubMed=19240079; DOI=10.1093/jac/dkp031;
RA Beresford N.J., Mulhearn D., Szczepankiewicz B., Liu G., Johnson M.E.,
RA Fordham-Skelton A., Abad-Zapatero C., Cavet J.S., Tabernero L.;
RT "Inhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs
RT mycobacterial survival in macrophages.";
RL J. Antimicrob. Chemother. 63:928-936(2009).
RN [9]
RP FUNCTION IN VIRULENCE, ACTIVITY REGULATION, BIOTECHNOLOGY, AND MUTAGENESIS
RP OF CYS-160.
RX PubMed=20167798; DOI=10.1073/pnas.0909133107;
RA Zhou B., He Y., Zhang X., Xu J., Luo Y., Wang Y., Franzblau S.G., Yang Z.,
RA Chan R.J., Liu Y., Zheng J., Zhang Z.Y.;
RT "Targeting mycobacterium protein tyrosine phosphatase B for
RT antituberculosis agents.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4573-4578(2010).
RN [10]
RP MUTAGENESIS OF PHE-161, AND FAMILY.
RX PubMed=20678187; DOI=10.1186/1471-2164-11-457;
RA Beresford N.J., Saville C., Bennett H.J., Roberts I.S., Tabernero L.;
RT "A new family of phosphoinositide phosphatases in microorganisms:
RT identification and biochemical analysis.";
RL BMC Genomics 11:457-457(2010).
RN [11]
RP ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RX PubMed=21116447; DOI=10.1021/ml1001135;
RA Chen L., Zhou B., Zhang S., Wu L., Wang Y., Franzblau S.G., Zhang Z.Y.;
RT "Identification and characterization of novel inhibitors of mPTPB, an
RT essential virulent phosphatase from Mycobacterium tuberculosis.";
RL ACS Med. Chem. Lett. 1:355-359(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [13]
RP BIOTECHNOLOGY.
RX PubMed=22136336; DOI=10.1021/jm2012062;
RA Chiaradia L.D., Martins P.G., Cordeiro M.N., Guido R.V., Ecco G.,
RA Andricopulo A.D., Yunes R.A., Vernal J., Nunes R.J., Terenzi H.;
RT "Synthesis, biological evaluation, and molecular modeling of chalcone
RT derivatives as potent inhibitors of Mycobacterium tuberculosis protein
RT tyrosine phosphatases (PtpA and PtpB).";
RL J. Med. Chem. 55:390-402(2012).
RN [14]
RP BIOTECHNOLOGY.
RX PubMed=24564493; DOI=10.1186/1471-2164-15-s1-s3;
RA Dhanjal J.K., Grover S., Sharma S., Singh A., Grover A.;
RT "Structural insights into mode of actions of novel natural Mycobacterium
RT protein tyrosine phosphatase B inhibitors.";
RL BMC Genomics 15:S3-S3(2014).
RN [15]
RP FUNCTION IN VIRULENCE.
RC STRAIN=H37Rv;
RX PubMed=29888212; DOI=10.3389/fcimb.2018.00171;
RA Fan L., Wu X., Jin C., Li F., Xiong S., Dong Y.;
RT "MptpB promotes mycobacteria survival by inhibiting the expression of
RT inflammatory mediators and cell apoptosis in macrophages.";
RL Front. Cell. Infect. Microbiol. 8:171-171(2018).
RN [16]
RP ACTIVITY REGULATION.
RX PubMed=30153005; DOI=10.1021/acs.jmedchem.8b00832;
RA Vickers C.F., Silva A.P.G., Chakraborty A., Fernandez P., Kurepina N.,
RA Saville C., Naranjo Y., Pons M., Schnettger L.S., Gutierrez M.G., Park S.,
RA Kreiswith B.N., Perlin D.S., Thomas E.J., Cavet J.S., Tabernero L.;
RT "Structure-based design of MptpB inhibitors that reduce multidrug-resistant
RT Mycobacterium tuberculosis survival and infection burden in vivo.";
RL J. Med. Chem. 61:8337-8352(2018).
RN [17]
RP REVIEW.
RX PubMed=23084287; DOI=10.1016/j.tim.2012.09.002;
RA Wong D., Chao J.D., Av-Gay Y.;
RT "Mycobacterium tuberculosis-secreted phosphatases: from pathogenesis to
RT targets for TB drug development.";
RL Trends Microbiol. 21:100-109(2013).
RN [18] {ECO:0007744|PDB:1YWF}
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND ACTIVE SITE.
RX PubMed=16271885; DOI=10.1016/j.str.2005.07.017;
RA Grundner C., Ng H.L., Alber T.;
RT "Mycobacterium tuberculosis protein tyrosine phosphatase PtpB structure
RT reveals a diverged fold and a buried active site.";
RL Structure 13:1625-1634(2005).
RN [19] {ECO:0007744|PDB:2OZ5}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR OMTS, AND
RP ACTIVITY REGULATION.
RX PubMed=17437721; DOI=10.1016/j.str.2007.03.003;
RA Grundner C., Perrin D., Hooft van Huijsduijnen R., Swinnen D., Gonzalez J.,
RA Gee C.L., Wells T.N., Alber T.;
RT "Structural basis for selective inhibition of Mycobacterium tuberculosis
RT protein tyrosine phosphatase PtpB.";
RL Structure 15:499-509(2007).
CC -!- FUNCTION: Essential virulence factor that promotes mycobacterial
CC survival within host macrophages (PubMed:14617138, PubMed:16256440,
CC PubMed:20167798, PubMed:29888212). Acts as a phosphatase that possesses
CC triple substrate specificity toward phosphotyrosine,
CC phosphoserine/threonine and phosphoinositides (PubMed:10986245,
CC PubMed:16271885, PubMed:17584180). Supports mycobacteria survival
CC during infection by modulating the normal host signaling pathways,
CC attenuating the bactericidal immune responses and promoting the host
CC cell survival (PubMed:20167798, PubMed:29888212). Inhibits host
CC inflammatory responses and apoptosis through impeding the NF-kappaB and
CC MAPK signal pathways and TP53/p53 expression in the macrophage
CC (PubMed:29888212). Blocks the IL6/IL-6 production by down-regulating
CC ERK1/2, p38 and p65 activity (PubMed:20167798, PubMed:29888212).
CC Prevents macrophage cell death by activating the Akt pathway and
CC blocking caspase 3 activity (PubMed:20167798, PubMed:29888212). Reduces
CC the expression of iNOS in activated macrophages and inhibits the
CC generation of destroying reactive nitrogen intermediate NO
CC (PubMed:29888212). {ECO:0000269|PubMed:10986245,
CC ECO:0000269|PubMed:14617138, ECO:0000269|PubMed:16256440,
CC ECO:0000269|PubMed:16271885, ECO:0000269|PubMed:17584180,
CC ECO:0000269|PubMed:20167798, ECO:0000269|PubMed:29888212}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:16271885,
CC ECO:0000269|PubMed:17584180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:16271885,
CC ECO:0000269|PubMed:17584180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:17584180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:17584180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:17584180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000269|PubMed:17584180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000269|PubMed:17584180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42329;
CC Evidence={ECO:0000269|PubMed:17584180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-4-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:45836, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:85468;
CC Evidence={ECO:0000269|PubMed:17584180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45837;
CC Evidence={ECO:0000269|PubMed:17584180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42308, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78911;
CC Evidence={ECO:0000269|PubMed:17584180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309;
CC Evidence={ECO:0000269|PubMed:17584180};
CC -!- ACTIVITY REGULATION: Phosphatase activity is inhibited by sodium
CC orthovanadate, a specific inhibitor of tyrosine phosphatases, but not
CC by okadaic acid, an inhibitor of serine/threonine phosphatases
CC (PubMed:10986245). Inhibition of the enzyme reduces mycobacterial
CC survival in infected macrophages (PubMed:19240079, PubMed:20167798,
CC PubMed:21116447, PubMed:30153005). Inhibitors also enhance killing
CC efficacy by first-line antibiotics (PubMed:30153005).
CC {ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:19240079,
CC ECO:0000269|PubMed:20167798, ECO:0000269|PubMed:21116447,
CC ECO:0000269|PubMed:30153005}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.291 mM for P-tyr {ECO:0000269|PubMed:17584180};
CC KM=0.44 mM for P-Ser {ECO:0000269|PubMed:17584180};
CC KM=0.253 mM for P-Thr {ECO:0000269|PubMed:17584180};
CC KM=0.217 mM for P-Tyr insulin {ECO:0000269|PubMed:17584180};
CC KM=0.327 mM for P-Tyr EGFR {ECO:0000269|PubMed:17584180};
CC KM=0.078 mM for P-Ser peptide {ECO:0000269|PubMed:17584180};
CC KM=0.076 mM for P-Thr peptide {ECO:0000269|PubMed:17584180};
CC KM=1.749 mM for 5'AMP {ECO:0000269|PubMed:17584180};
CC KM=1.196 mM for 5'IMP {ECO:0000269|PubMed:17584180};
CC KM=0.170 mM for pNPP {ECO:0000269|PubMed:17584180};
CC KM=10 mM for pNPP {ECO:0000269|PubMed:16271885};
CC KM=0.018 mM for PtdIns3P {ECO:0000269|PubMed:17584180};
CC KM=0.074 mM for PtdIns4P {ECO:0000269|PubMed:17584180};
CC KM=0.064 mM for PtdIns5P {ECO:0000269|PubMed:17584180};
CC Note=kcat is 60.0 sec(-1) with P-Tyr as substrate. kcat is 18.32
CC sec(-1) with P-Ser as substrate. kcat is 12.5 sec(-1) with P-Thr as
CC substrate. kcat is 159.57 sec(-1) with P-Tyr insulin as substrate.
CC kcat is 158.31 sec(-1) with P-Tyr EGFR as substrate. kcat is 18.08
CC sec(-1) with P-Ser peptide as substrate. kcat is 9.12 sec(-1) with P-
CC Thr peptide as substrate. kcat is 60.97 sec(-1) with 5'AMP as
CC substrate. kcat is 88.40 sec(-1) with 5'IMP as substrate. kcat is
CC 134.70 sec(-1) with pNPP as substrate. kcat is 38.5 sec(-1) with
CC PtdIns3P as substrate. kcat is 100.3 sec(-1) with PtdIns4P as
CC substrate. kcat is 80.5 sec(-1) with PtdIns5P as substrate.
CC {ECO:0000269|PubMed:17584180};
CC pH dependence:
CC Optimum pH is near 5.5. {ECO:0000269|PubMed:16271885};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10986245}.
CC Note=Further investigation is required to determine whether PtpB is
CC direct substrate for SecA2, the ESX/type VII secretion system, or an
CC alternate mechanism. {ECO:0000305|PubMed:23084287}.
CC -!- DOMAIN: Adopts a simplified PTP fold, which combines features of the
CC conventional PTPs and dual-specificity phosphatases (PubMed:16271885).
CC In the presence of OMTS inhibitor, the enzyme undergoes a large
CC conformational change, allowing the inhibitor to bind deep in the
CC active-site pocket (PubMed:17437721). {ECO:0000269|PubMed:16271885,
CC ECO:0000269|PubMed:17437721}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene impairs the ability of the
CC mutant strain to survive in activated murine macrophages and in guinea
CC pigs, but not in resting murine macrophages (PubMed:14617138,
CC PubMed:16256440). Infection of guinea pigs with the mutant strain
CC results in a 70-fold reduction in the bacillary load of spleens in
CC infected animals (PubMed:14617138, PubMed:16256440). Disruption of the
CC gene has no significant effect on the morphology and growth of the
CC mutant in defined liquid culture medium (PubMed:14617138).
CC {ECO:0000269|PubMed:14617138, ECO:0000269|PubMed:16256440}.
CC -!- BIOTECHNOLOGY: The important role played by PtpB in virulence and the
CC lack of PtpB human orthologs make it a highly promising target for the
CC treatment of tuberculosis infections. Several classes of potent
CC inhibitors have been developed and studied to date. Drug candidates
CC include, among others, (oxalylamino-methylene)-thiophene sulfonamide
CC (OMTS), isoxazole-based compounds, highly substituted indolo[2,3-
CC a]quinolizidines, benzofuran salicylic acid derivatives, chalcone
CC derivatives and several 2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamide
CC and piperazinyl-thiophenyl-ethyl-oxalamide derivatives.
CC {ECO:0000269|PubMed:17437721, ECO:0000269|PubMed:17636914,
CC ECO:0000269|PubMed:17685373, ECO:0000269|PubMed:19240079,
CC ECO:0000269|PubMed:20167798, ECO:0000269|PubMed:21116447,
CC ECO:0000269|PubMed:22136336, ECO:0000269|PubMed:24564493}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42878.1; -; Genomic_DNA.
DR RefSeq; NP_214667.1; NC_000962.3.
DR RefSeq; WP_003401010.1; NZ_NVQJ01000001.1.
DR PDB; 1YWF; X-ray; 1.71 A; A=1-276.
DR PDB; 2OZ5; X-ray; 2.00 A; A/B=1-276.
DR PDBsum; 1YWF; -.
DR PDBsum; 2OZ5; -.
DR AlphaFoldDB; I6WXK4; -.
DR SMR; I6WXK4; -.
DR STRING; 83332.Rv0153c; -.
DR SwissLipids; SLP:000001160; -.
DR PaxDb; I6WXK4; -.
DR PRIDE; I6WXK4; -.
DR DNASU; 886842; -.
DR GeneID; 886842; -.
DR KEGG; mtu:Rv0153c; -.
DR PATRIC; fig|83332.111.peg.178; -.
DR TubercuList; Rv0153c; -.
DR eggNOG; COG2365; Bacteria.
DR OMA; HTIFDFR; -.
DR PhylomeDB; I6WXK4; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR026893; Tyr/Ser_Pase_IphP-type.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF13350; Y_phosphatase3; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protein phosphatase; Reference proteome; Secreted;
KW Virulence.
FT CHAIN 1..276
FT /note="Triple specificity protein phosphatase PtpB"
FT /id="PRO_0000450734"
FT ACT_SITE 160
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305|PubMed:16271885,
FT ECO:0000305|PubMed:17584180"
FT SITE 164
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:17584180"
FT SITE 165
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:17584180"
FT MUTAGEN 82
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:17584180"
FT MUTAGEN 160
FT /note="C->S: Shows less than 1% of wild-type activity. Does
FT not affect macrophage apoptosis."
FT /evidence="ECO:0000269|PubMed:10986245,
FT ECO:0000269|PubMed:17584180, ECO:0000269|PubMed:20167798"
FT MUTAGEN 161
FT /note="F->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20678187"
FT MUTAGEN 161
FT /note="F->K: Shows new activity for di-phosphorylated
FT substrates PI(3,4)P2, PI(4,5)P2 and PI(3,4,5)P3."
FT /evidence="ECO:0000269|PubMed:20678187"
FT MUTAGEN 164
FT /note="K->A: Shows less than 10% of the wild-type activity
FT towards phosphotyrosine peptides, but remains unaltered
FT towards pNPP and phosphoserine/threonine peptides."
FT /evidence="ECO:0000269|PubMed:17584180"
FT MUTAGEN 165
FT /note="D->N: Shows less than 0.1% of wild-type activity
FT with peptides substrates."
FT /evidence="ECO:0000269|PubMed:17584180"
FT MUTAGEN 166
FT /note="R->A: Shows less than 1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17584180"
SQ SEQUENCE 276 AA; 30154 MW; 2794F56866D2E432 CRC64;
MAVRELPGAW NFRDVADTAT ALRPGRLFRS SELSRLDDAG RATLRRLGIT DVADLRSSRE
VARRGPGRVP DGIDVHLLPF PDLADDDADD SAPHETAFKR LLTNDGSNGE SGESSQSIND
AATRYMTDEY RQFPTRNGAQ RALHRVVTLL AAGRPVLTHC FAGKDRTGFV VALVLEAVGL
DRDVIVADYL RSNDSVPQLR ARISEMIQQR FDTELAPEVV TFTKARLSDG VLGVRAEYLA
AARQTIDETY GSLGGYLRDA GISQATVNRM RGVLLG
