ID   WZB_ECO57               Reviewed;         147 AA.
AC   P0AAB3; P77153;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase Wzb;
DE            EC=3.1.3.48;
GN   Name=wzb; OrderedLocusNames=Z3226, ECs2866;
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 Wzc. Required for the extracellular
CC       polysaccharide colanic acid synthesis. Probably involved in the export
CC       of colanic acid from the cell to medium. Involved in protection of
CC       cells against contact-dependent growth inhibition (CDI).
CC       {ECO:0000250|UniProtKB:P0AAB2}.
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   -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
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; AE005174; AAG57121.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36289.1; -; Genomic_DNA.
DR   PIR; B90987; B90987.
DR   PIR; E85832; E85832.
DR   RefSeq; NP_310893.1; NC_002695.1.
DR   RefSeq; WP_000482901.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AAB3; -.
DR   BMRB; P0AAB3; -.
DR   SMR; P0AAB3; -.
DR   STRING; 155864.EDL933_3134; -.
DR   EnsemblBacteria; AAG57121; AAG57121; Z3226.
DR   EnsemblBacteria; BAB36289; BAB36289; ECs_2866.
DR   GeneID; 67417846; -.
DR   GeneID; 913690; -.
DR   KEGG; ece:Z3226; -.
DR   KEGG; ecs:ECs_2866; -.
DR   PATRIC; fig|386585.9.peg.2999; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_1_1_6; -.
DR   OMA; YQQVTRF; -.
DR   UniPathway; UPA00631; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
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   Exopolysaccharide synthesis; Hydrolase; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..147
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   Wzb"
FT                   /id="PRO_0000046573"
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        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   147 AA;  16709 MW;  6E36D7CE1038133B CRC64;
     MFNNILVVCV GNICRSPTAE RLLQRYHPEL KVESAGLGAL VGKGADPTAI SVAAEHQLSL
     EGHCARQISR RLCRNYDLIL TMEKRHIERL CEMAPEMRGK VMLFGHWDNE CEIPDPYRKS
     RETFAAVYTL LERSARQWAQ ALNAEQV