ID   PTPA_STRCO              Reviewed;         164 AA.
AC   P53433;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase;
DE            Short=PTPase;
DE            EC=3.1.3.48;
DE   AltName: Full=Small, acidic phosphotyrosine protein phosphatase;
DE            Short=PY protein phosphatase;
GN   Name=ptpA; OrderedLocusNames=SCO3921; ORFNames=SCQ11.04c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / 1147;
RX   PubMed=8550407; DOI=10.1128/jb.178.1.136-142.1996;
RA   Li Y., Strohl W.R.;
RT   "Cloning, purification, and properties of a phosphotyrosine protein
RT   phosphatase from Streptomyces coelicolor A3(2).";
RL   J. Bacteriol. 178:136-142(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
CC       phosphates and natural and synthetic acyl phosphates. May be involved
CC       in the regulation of sulfur amino acid metabolism.
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}.
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; U37580; AAC43614.1; -; Genomic_DNA.
DR   EMBL; AL939118; CAB46959.1; -; Genomic_DNA.
DR   PIR; T37174; T37174.
DR   RefSeq; NP_628106.1; NC_003888.3.
DR   RefSeq; WP_003975011.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; P53433; -.
DR   SMR; P53433; -.
DR   STRING; 100226.SCO3921; -.
DR   GeneID; 1099357; -.
DR   KEGG; sco:SCO3921; -.
DR   PATRIC; fig|100226.15.peg.3995; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_2_1_11; -.
DR   InParanoid; P53433; -.
DR   OMA; TGSWHVG; -.
DR   PhylomeDB; P53433; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..164
FT                   /note="Low molecular weight protein-tyrosine-phosphatase"
FT                   /id="PRO_0000046569"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   164 AA;  17690 MW;  56A4AC5D644771F9 CRC64;
     MTYRVCFVCT GNICRSPMAE AVFRARVEDA GLGHLVEADS AGTGGWHEGE GADPRTEAVL
     ADHGYGLDHA ARQFQQSWFS RLDLVVALDA GHLRALRRLA PTERDAAKVR LLRSYDPAVA
     GGDLDVPDPY YGGRDGFEEC LEMVEAASTG LLAAVREQVE GRAA