ID   PTPA_MYCTO              Reviewed;         163 AA.
AC   P9WIA0; L0TAK9; P65716; Q10507;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Low molecular weight protein-tyrosine phosphatase A {ECO:0000250|UniProtKB:P9WIA1};
DE            Short=LMW-PTP {ECO:0000250|UniProtKB:P9WIA1};
DE            Short=PTPase {ECO:0000250|UniProtKB:P9WIA1};
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:P9WIA1};
DE   AltName: Full=Low molecular weight tyrosine phosphatase PtpA {ECO:0000250|UniProtKB:P9WIA1};
GN   Name=ptpA; OrderedLocusNames=MT2293;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Key virulence factor required for mycobacterial survival
CC       within host macrophages (By similarity). Exhibits protein tyrosine
CC       phosphatase activity (By similarity). {ECO:0000250|UniProtKB:P9WIA1}.
CC   -!- FUNCTION: Supports mycobacteria survival during infection by modulation
CC       of the phagosome maturation and modulation of the normal host signaling
CC       pathways, including host innate immune responses and cell apoptosis.
CC       {ECO:0000250|UniProtKB:P9WIA1}.
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:0000250|UniProtKB:P9WIA1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000250|UniProtKB:P9WIA1};
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46577.1; -; Genomic_DNA.
DR   PIR; F70777; F70777.
DR   RefSeq; WP_003411510.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIA0; -.
DR   BMRB; P9WIA0; -.
DR   SMR; P9WIA0; -.
DR   EnsemblBacteria; AAK46577; AAK46577; MT2293.
DR   GeneID; 45426212; -.
DR   KEGG; mtc:MT2293; -.
DR   PATRIC; fig|83331.31.peg.2470; -.
DR   HOGENOM; CLU_071415_2_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase; Virulence.
FT   CHAIN           1..163
FT                   /note="Low molecular weight protein-tyrosine phosphatase A"
FT                   /id="PRO_0000428043"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIA1"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000250|UniProtKB:P9WIA1"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIA1"
SQ   SEQUENCE   163 AA;  17892 MW;  9D1CF0DB24CA8E27 CRC64;
     MSDPLHVTFV CTGNICRSPM AEKMFAQQLR HRGLGDAVRV TSAGTGNWHV GSCADERAAG
     VLRAHGYPTD HRAAQVGTEH LAADLLVALD RNHARLLRQL GVEAARVRML RSFDPRSGTH
     ALDVEDPYYG DHSDFEEVFA VIESALPGLH DWVDERLARN GPS