ID   PTPA_STAAB              Reviewed;         154 AA.
AC   Q2YU46;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SAB1813;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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: Phosophorylations 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}.
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DR   EMBL; AJ938182; CAI81502.1; -; Genomic_DNA.
DR   RefSeq; WP_000228664.1; NC_007622.1.
DR   AlphaFoldDB; Q2YU46; -.
DR   SMR; Q2YU46; -.
DR   KEGG; sab:SAB1813; -.
DR   HOGENOM; CLU_071415_2_3_9; -.
DR   OMA; TGSWHVG; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Phosphoprotein; Protein phosphatase; Secreted.
FT   CHAIN           1..154
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpA"
FT                   /id="PRO_0000300657"
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;  17551 MW;  67E81E1E9425A4FD CRC64;
     MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP HEGTQKILNK
     HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKFINPNL KGQLFKLLEF SNMEESDVPD
     PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN LKEG