ETP_ECOLI
ID ETP_ECOLI Reviewed; 148 AA.
AC P0ACZ2; P75880; Q8XC24;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Low molecular weight protein-tyrosine-phosphatase Etp;
DE EC=3.1.3.48;
GN Name=etp; Synonyms=yccY; OrderedLocusNames=b0982, JW5132;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11090276; DOI=10.1006/jmbi.2000.4217;
RA Vincent C., Duclos B., Grangeasse C., Vaganay E., Riberty M., Cozzone A.J.,
RA Doublet P.;
RT "Relationship between exopolysaccharide production and protein-tyrosine
RT phosphorylation in Gram-negative bacteria.";
RL J. Mol. Biol. 304:311-321(2000).
CC -!- FUNCTION: Dephosphorylates etk.
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 -!- CAUTION: In E.coli K12 / MG1655 and K12 / W3110 this operon is silenced
CC by an IS1D insertion in the promoter region. {ECO:0000305}.
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DR EMBL; U00096; AAC74067.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35747.2; -; Genomic_DNA.
DR PIR; D64839; D64839.
DR RefSeq; NP_415502.4; NC_000913.3.
DR RefSeq; WP_000057871.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P0ACZ2; -.
DR SMR; P0ACZ2; -.
DR BioGRID; 4261407; 378.
DR STRING; 511145.b0982; -.
DR PaxDb; P0ACZ2; -.
DR PRIDE; P0ACZ2; -.
DR EnsemblBacteria; AAC74067; AAC74067; b0982.
DR EnsemblBacteria; BAA35747; BAA35747; BAA35747.
DR GeneID; 66670741; -.
DR GeneID; 945236; -.
DR KEGG; ecj:JW5132; -.
DR KEGG; eco:b0982; -.
DR PATRIC; fig|1411691.4.peg.1291; -.
DR EchoBASE; EB3491; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_1_1_6; -.
DR InParanoid; P0ACZ2; -.
DR OMA; AFFPQKA; -.
DR PhylomeDB; P0ACZ2; -.
DR BioCyc; EcoCyc:G6503-MON; -.
DR BioCyc; MetaCyc:G6503-MON; -.
DR PRO; PR:P0ACZ2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:EcoCyc.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:EcoCyc.
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 Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..148
FT /note="Low molecular weight protein-tyrosine-phosphatase
FT Etp"
FT /id="PRO_0000046576"
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
