ID   PTPA_STAAS              Reviewed;         154 AA.
AC   Q6G853;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase PtpA;
DE            EC=3.1.3.48;
DE   AltName: Full=Phosphotyrosine phosphatase A;
DE            Short=PTPase A;
GN   Name=ptpA; OrderedLocusNames=SAS1803;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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: Secreted tyrosine phosphatase that plays a critical role
CC       during infection as a bacterial effector protein that counteracts host
CC       defenses. Required for intramacrophage survival.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
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:A0A0H3K9F2};
CC   -!- SUBUNIT: Interacts with host CORO1A.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC       Note=Secreted intracellularly upon bacterial infection of macrophages.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- PTM: Phosphorylations at Tyr-122 and Tyr-123 are essential for
CC       phosphatase activity. {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG43608.1; -; Genomic_DNA.
DR   RefSeq; WP_000228666.1; NC_002953.3.
DR   AlphaFoldDB; Q6G853; -.
DR   SMR; Q6G853; -.
DR   KEGG; sas:SAS1803; -.
DR   HOGENOM; CLU_071415_2_3_9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd16343; LMWPTP; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   PANTHER; PTHR11717:SF7; LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11717; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; 1.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Phosphoprotein; Protein phosphatase; Secreted.
FT   CHAIN           1..154
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpA"
FT                   /id="PRO_0000300660"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        14
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   154 AA;  17491 MW;  67E81E0B8125B1E8 CRC64;
     MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP HEGTQKILNK
     HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKSINPNL KGQLFKLLEF SNMEESDVPD
     PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN LKEG
//