ID   PTPB_STAAR              Reviewed;         139 AA.
AC   Q6GEW0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase PtpB;
DE            EC=3.1.3.48;
DE   AltName: Full=Phosphotyrosine phosphatase B;
DE            Short=PTPase B;
GN   Name=ptpB; OrderedLocusNames=SAR2203;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Dephosphorylates the phosphotyrosine-containing proteins.
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG41184.1; -; Genomic_DNA.
DR   RefSeq; WP_000697334.1; NC_002952.2.
DR   AlphaFoldDB; Q6GEW0; -.
DR   SMR; Q6GEW0; -.
DR   KEGG; sar:SAR2203; -.
DR   HOGENOM; CLU_071415_1_2_9; -.
DR   OMA; AFFPQKA; -.
DR   OrthoDB; 2062716at2; -.
DR   Proteomes; UP000000596; 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.
FT   CHAIN           1..139
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpB"
FT                   /id="PRO_0000300673"
FT   ACT_SITE        7
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        13
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   139 AA;  15788 MW;  63EB2C0E2A53EA5B CRC64;
     MKILFVCTGN TCRSPLAESI AKEVMPNHQF ESRGIFAVNN QGVSNYVEDL VEEHHLAETT
     LSQQFTEADL KADIILTMSY SHKELIEAHF GLQNHVFTLH EYVKEAGEVI DPYGGTKEMY
     VHTYEELVSL ILKLKDIIC