ID   WZB_SALTY               Reviewed;         149 AA.
AC   Q9F7B2;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase Wzb;
DE            EC=3.1.3.48;
GN   Name=wzb; OrderedLocusNames=STM2117;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=11004393; DOI=10.1111/j.1574-6968.2000.tb09312.x;
RA   Stevenson G., Lan R., Reeves P.R.;
RT   "The colanic acid gene cluster of Salmonella enterica has a complex
RT   history.";
RL   FEMS Microbiol. Lett. 191:11-16(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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}.
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DR   EMBL; AF285084; AAG24805.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21021.1; -; Genomic_DNA.
DR   RefSeq; NP_461062.1; NC_003197.2.
DR   RefSeq; WP_000482224.1; NC_003197.2.
DR   AlphaFoldDB; Q9F7B2; -.
DR   SMR; Q9F7B2; -.
DR   STRING; 99287.STM2117; -.
DR   PaxDb; Q9F7B2; -.
DR   EnsemblBacteria; AAL21021; AAL21021; STM2117.
DR   GeneID; 1253638; -.
DR   KEGG; stm:STM2117; -.
DR   PATRIC; fig|99287.12.peg.2239; -.
DR   HOGENOM; CLU_071415_1_1_6; -.
DR   OMA; YQQVTRF; -.
DR   PhylomeDB; Q9F7B2; -.
DR   BioCyc; SENT99287:STM2117-MON; -.
DR   UniPathway; UPA00631; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
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..149
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   Wzb"
FT                   /id="PRO_0000046575"
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;  16474 MW;  DA5DF9B5699EF208 CRC64;
     MFNKILVVCV GNVCRSPTAE RLLKRFHPSL TVASAGLGAL VGKGADPAAA SVASAHDLSL
     ENHCARQISA RLCREYDLIL TMEKRHIAAL CDIAPEMRGK VMLFGHWDSE REIPDPYRKS
     RDAFEAVYTL LERSARQWAQ ALNAEQGKP