ETP_ECO57
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 03-AUG-2022, entry version 91.
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; Proteobacteria; 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_SWKA01000005.1.
DR AlphaFoldDB; P0ACZ3; -.
DR SMR; P0ACZ3; -.
DR STRING; 155864.EDL933_1320; -.
DR EnsemblBacteria; AAG55530; AAG55530; Z1399.
DR EnsemblBacteria; BAB34561; BAB34561; ECs_1138.
DR GeneID; 66670741; -.
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 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..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