ID   PTPA_STAAU              Reviewed;         154 AA.
AC   P0C5D2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Reynolds;
RX   PubMed=12193638; DOI=10.1128/jb.184.18.5194-5199.2002;
RA   Soulat D., Vaganay E., Duclos B., Genestier A.-L., Etienne J.,
RA   Cozzone A.J.;
RT   "Staphylococcus aureus contains two low-molecular-mass phosphotyrosine
RT   protein phosphatases.";
RL   J. Bacteriol. 184:5194-5199(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 1-152.
RX   PubMed=21871460; DOI=10.1016/j.jmb.2011.08.015;
RA   Vega C., Chou S., Engel K., Harrell M.E., Rajagopal L., Grundner C.;
RT   "Structure and substrate recognition of the Staphylococcus aureus protein
RT   tyrosine phosphatase PtpA.";
RL   J. Mol. Biol. 413:24-31(2011).
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:0000269|PubMed:12193638};
CC   -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and sodium
CC       orthovanadate. {ECO:0000269|PubMed:12193638}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.2 mM for p-nitrophenyl-phosphate (at pH 6.2 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:12193638};
CC         Vmax=33.6 umol/min/mg enzyme (at pH 6.2 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:12193638};
CC       pH dependence:
CC         Optimum pH is 6.2. {ECO:0000269|PubMed:12193638};
CC       Temperature dependence:
CC         Optimum temperature is about 40 degrees Celsius.
CC         {ECO:0000269|PubMed:12193638};
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   RefSeq; WP_000228666.1; NZ_WYDB01000009.1.
DR   PDB; 3ROF; X-ray; 1.03 A; A=1-152.
DR   PDBsum; 3ROF; -.
DR   AlphaFoldDB; P0C5D2; -.
DR   SMR; P0C5D2; -.
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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Phosphoprotein; Protein phosphatase; Secreted.
FT   CHAIN           1..154
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpA"
FT                   /id="PRO_0000300656"
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"
FT   STRAND          2..13
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   HELIX           14..28
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   STRAND          80..86
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   HELIX           87..96
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:3ROF"
FT   HELIX           127..148
FT                   /evidence="ECO:0007829|PDB:3ROF"
SQ   SEQUENCE   154 AA;  17491 MW;  67E81E0B8125B1E8 CRC64;
     MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP HEGTQKILNK
     HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKSINPNL KGQLFKLLEF SNMEESDVPD
     PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN LKEG