ID   WZB_SALTI               Reviewed;         149 AA.
AC   Q8Z5G5;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase Wzb;
DE            EC=3.1.3.48;
GN   Name=wzb; OrderedLocusNames=STY2330, t0755;
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
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DR   EMBL; AL513382; CAD02480.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68448.1; -; Genomic_DNA.
DR   RefSeq; NP_456663.1; NC_003198.1.
DR   RefSeq; WP_000482225.1; NZ_WSUR01000002.1.
DR   AlphaFoldDB; Q8Z5G5; -.
DR   SMR; Q8Z5G5; -.
DR   STRING; 220341.gene:17586235; -.
DR   KEGG; stt:t0755; -.
DR   KEGG; sty:STY2330; -.
DR   PATRIC; fig|220341.7.peg.2351; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_1_1_6; -.
DR   OMA; QGEWHVE; -.
DR   OrthoDB; 9784339at2; -.
DR   UniPathway; UPA00631; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   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   Exopolysaccharide synthesis; Hydrolase; Protein phosphatase.
FT   CHAIN           1..149
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   Wzb"
FT                   /id="PRO_0000046574"
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   149 AA;  16504 MW;  DA5DE2C3B2E83208 CRC64;
     MFNKILVVCV GNVCRSPTAE RLLKRFHPSL TVASAGLGAL VGKGADPAAA SVASAHDLSL
     ENHCARQISA RLCREYDLIL TMEKRHIAAL CDIAPEMRSK VMLFGHWDSE REIPDPYRKS
     RDAFEAVYTL LERSARQWAQ ALNAEQGKP
//