ID   ETP_ECO57               Reviewed;         148 AA.
AC   P0ACZ3; P75880; Q8XC24;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase Etp;
DE            EC=3.1.3.48;
GN   Name=etp; OrderedLocusNames=Z1399, ECs1138;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Dephosphorylates etk. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG55530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB34561.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG55530.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB34561.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_309165.2; NC_002695.1.
DR   RefSeq; WP_000057871.1; NZ_VOAI01000025.1.
DR   AlphaFoldDB; P0ACZ3; -.
DR   SMR; P0ACZ3; -.
DR   STRING; 155864.Z1399; -.
DR   GeneID; 75171057; -.
DR   GeneID; 914076; -.
DR   KEGG; ece:Z1399; -.
DR   KEGG; ecs:ECs_1138; -.
DR   PATRIC; fig|386585.9.peg.1254; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_1_1_6; -.
DR   OMA; AFFPQKA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; Protein phosphatase; Reference proteome.
FT   CHAIN           1..148
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   Etp"
FT                   /id="PRO_0000046577"
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   148 AA;  16386 MW;  136DA7AEF6AE8F0C CRC64;
     MAQLKFNSIL VVCTGNICRS PIGERLLRKR LPGVKVKSAG VHGLVKHPAD ATAADVAANH
     GVSLEGHAGR KLTAEMARNY DLILAMESEH IAQVTAIAPE VRGKTMLFGQ WLEQKEIPDP
     YRKSQDAFEH VYGMLERASQ EWAKRLSR
//