WZB_ECOLI
ID WZB_ECOLI Reviewed; 147 AA.
AC P0AAB2; P77153; Q2MAY1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Low molecular weight protein-tyrosine-phosphatase Wzb;
DE EC=3.1.3.48 {ECO:0000269|PubMed:10348860};
GN Name=wzb; OrderedLocusNames=b2061, JW2046;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8759852; DOI=10.1128/jb.178.16.4885-4893.1996;
RA Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.;
RT "Organization of the Escherichia coli K-12 gene cluster responsible for
RT production of the extracellular polysaccharide colanic acid.";
RL J. Bacteriol. 178:4885-4893(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 FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10348860; DOI=10.1128/jb.181.11.3472-3477.1999;
RA Vincent C., Doublet P., Grangeasse C., Vaganay E., Cozzone A.J., Duclos B.;
RT "Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a
RT phosphotyrosine-protein phosphatase, Wzb.";
RL J. Bacteriol. 181:3472-3477(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061, and K12 / MC4100;
RX PubMed=18761695; DOI=10.1111/j.1365-2958.2008.06404.x;
RA Aoki S.K., Malinverni J.C., Jacoby K., Thomas B., Pamma R., Trinh B.N.,
RA Remers S., Webb J., Braaten B.A., Silhavy T.J., Low D.A.;
RT "Contact-dependent growth inhibition requires the essential outer membrane
RT protein BamA (YaeT) as the receptor and the inner membrane transport
RT protein AcrB.";
RL Mol. Microbiol. 70:323-340(2008).
CC -!- FUNCTION: Dephosphorylates Wzc (PubMed:10348860). Required for the
CC extracellular polysaccharide colanic acid synthesis, probably involved
CC in the export of colanic acid from the cell to medium
CC (PubMed:11090276). Involved in protection of cells against contact-
CC dependent growth inhibition (CDI), probably due to the loss of a
CC physical impediment to cell-cell contact. {ECO:0000269|PubMed:10348860,
CC ECO:0000269|PubMed:11090276, ECO:0000269|PubMed:18761695}.
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 Evidence={ECO:0000269|PubMed:10348860};
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- DISRUPTION PHENOTYPE: No phosphorylation of Wzc (PubMed:11090276). Loss
CC of mucoid colony phenotype, greatly increased susceptibility to
CC contact-dependent growth inhibition (CDI) (PubMed:18761695).
CC {ECO:0000269|PubMed:11090276, ECO:0000269|PubMed:18761695}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; U38473; AAC77834.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75122.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76575.1; -; Genomic_DNA.
DR PIR; D64972; D64972.
DR RefSeq; NP_416565.1; NC_000913.3.
DR RefSeq; WP_000482901.1; NZ_STEB01000002.1.
DR PDB; 2FEK; NMR; -; A=1-147.
DR PDBsum; 2FEK; -.
DR AlphaFoldDB; P0AAB2; -.
DR BMRB; P0AAB2; -.
DR SMR; P0AAB2; -.
DR BioGRID; 4260957; 423.
DR IntAct; P0AAB2; 17.
DR MINT; P0AAB2; -.
DR STRING; 511145.b2061; -.
DR PaxDb; P0AAB2; -.
DR PRIDE; P0AAB2; -.
DR EnsemblBacteria; AAC75122; AAC75122; b2061.
DR EnsemblBacteria; BAE76575; BAE76575; BAE76575.
DR GeneID; 67417846; -.
DR GeneID; 946564; -.
DR KEGG; ecj:JW2046; -.
DR KEGG; eco:b2061; -.
DR PATRIC; fig|511145.12.peg.2138; -.
DR EchoBASE; EB3337; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_1_1_6; -.
DR InParanoid; P0AAB2; -.
DR OMA; YQQVTRF; -.
DR PhylomeDB; P0AAB2; -.
DR BioCyc; EcoCyc:G7106-MON; -.
DR BioCyc; MetaCyc:G7106-MON; -.
DR UniPathway; UPA00631; -.
DR EvolutionaryTrace; P0AAB2; -.
DR PRO; PR:P0AAB2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:EcoCyc.
DR GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000046572"
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"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2FEK"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2FEK"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:2FEK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2FEK"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2FEK"
FT HELIX 121..143
FT /evidence="ECO:0007829|PDB:2FEK"
SQ SEQUENCE 147 AA; 16709 MW; 6E36D7CE1038133B CRC64;
MFNNILVVCV GNICRSPTAE RLLQRYHPEL KVESAGLGAL VGKGADPTAI SVAAEHQLSL
EGHCARQISR RLCRNYDLIL TMEKRHIERL CEMAPEMRGK VMLFGHWDNE CEIPDPYRKS
RETFAAVYTL LERSARQWAQ ALNAEQV
