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Protein

Low molecular weight protein-tyrosine-phosphatase Wzb

Gene

wzb

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Dephosphorylates Wzc (PubMed:10348860). Required for the extracellular polysaccharide colanic acid synthesis, probably involved in the export of colanic acid from the cell to medium (PubMed:11090276). Involved in protection of cells against contact-dependent growth inhibition (CDI), probably due to the loss of a physical impediment to cell-cell contact.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Pathway: exopolysaccharide biosynthesis

This protein is involved in the pathway exopolysaccharide biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway exopolysaccharide biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91NucleophileBy similarity
Active sitei14 – 141By similarity
Active sitei115 – 1151Proton donorBy similarity

GO - Molecular functioni

  • protein tyrosine phosphatase activity Source: EcoCyc

GO - Biological processi

  • colanic acid biosynthetic process Source: EcoCyc
  • peptidyl-tyrosine dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Exopolysaccharide synthesis

Enzyme and pathway databases

BioCyciEcoCyc:G7106-MONOMER.
ECOL316407:JW2046-MONOMER.
MetaCyc:G7106-MONOMER.
UniPathwayiUPA00631.

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight protein-tyrosine-phosphatase Wzb (EC:3.1.3.481 Publication)
Gene namesi
Name:wzb
Ordered Locus Names:b2061, JW2046
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13567. wzb.

Pathology & Biotechi

Disruption phenotypei

No phosphorylation of Wzc (PubMed:11090276). Loss of mucoid colony phenotype, greatly increased susceptibility to contact-dependent growth inhibition (CDI) (PubMed:18761695).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Low molecular weight protein-tyrosine-phosphatase WzbPRO_0000046572Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP0AAB2. 17 interactions.
MINTiMINT-8293227.
STRINGi511145.b2061.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411Combined sources
Helixi15 – 2612Combined sources
Beta strandi31 – 366Combined sources
Helixi47 – 559Combined sources
Helixi70 – 756Combined sources
Beta strandi76 – 827Combined sources
Helixi84 – 9310Combined sources
Helixi95 – 1006Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 1074Combined sources
Turni108 – 1103Combined sources
Helixi121 – 14323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FEKNMR-A1-147[»]
ProteinModelPortaliP0AAB2.
SMRiP0AAB2. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AAB2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
HOGENOMiHOG000273091.
InParanoidiP0AAB2.
KOiK01104.
OMAiCEIAPEM.
OrthoDBiEOG63VC26.
PhylomeDBiP0AAB2.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AAB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNNILVVCV GNICRSPTAE RLLQRYHPEL KVESAGLGAL VGKGADPTAI
60 70 80 90 100
SVAAEHQLSL EGHCARQISR RLCRNYDLIL TMEKRHIERL CEMAPEMRGK
110 120 130 140
VMLFGHWDNE CEIPDPYRKS RETFAAVYTL LERSARQWAQ ALNAEQV
Length:147
Mass (Da):16,709
Last modified:September 13, 2005 - v1
Checksum:i6E36D7CE1038133B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38473 Genomic DNA. Translation: AAC77834.1.
U00096 Genomic DNA. Translation: AAC75122.1.
AP009048 Genomic DNA. Translation: BAE76575.1.
PIRiD64972.
RefSeqiNP_416565.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75122; AAC75122; b2061.
BAE76575; BAE76575; BAE76575.
GeneIDi946564.
KEGGiecj:Y75_p2024.
eco:b2061.
PATRICi32119455. VBIEscCol129921_2138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38473 Genomic DNA. Translation: AAC77834.1.
U00096 Genomic DNA. Translation: AAC75122.1.
AP009048 Genomic DNA. Translation: BAE76575.1.
PIRiD64972.
RefSeqiNP_416565.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FEKNMR-A1-147[»]
ProteinModelPortaliP0AAB2.
SMRiP0AAB2. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0AAB2. 17 interactions.
MINTiMINT-8293227.
STRINGi511145.b2061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75122; AAC75122; b2061.
BAE76575; BAE76575; BAE76575.
GeneIDi946564.
KEGGiecj:Y75_p2024.
eco:b2061.
PATRICi32119455. VBIEscCol129921_2138.

Organism-specific databases

EchoBASEiEB3337.
EcoGeneiEG13567. wzb.

Phylogenomic databases

eggNOGiCOG0394.
HOGENOMiHOG000273091.
InParanoidiP0AAB2.
KOiK01104.
OMAiCEIAPEM.
OrthoDBiEOG63VC26.
PhylomeDBiP0AAB2.

Enzyme and pathway databases

UniPathwayiUPA00631.
BioCyciEcoCyc:G7106-MONOMER.
ECOL316407:JW2046-MONOMER.
MetaCyc:G7106-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AAB2.
PROiP0AAB2.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid."
    Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.
    J. Bacteriol. 178:4885-4893(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a phosphotyrosine-protein phosphatase, Wzb."
    Vincent C., Doublet P., Grangeasse C., Vaganay E., Cozzone A.J., Duclos B.
    J. Bacteriol. 181:3472-3477(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: K12 / JM109 / ATCC 53323.
  5. "Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in Gram-negative bacteria."
    Vincent C., Duclos B., Grangeasse C., Vaganay E., Riberty M., Cozzone A.J., Doublet P.
    J. Mol. Biol. 304:311-321(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / JM109 / ATCC 53323.
  6. "Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB."
    Aoki S.K., Malinverni J.C., Jacoby K., Thomas B., Pamma R., Trinh B.N., Remers S., Webb J., Braaten B.A., Silhavy T.J., Low D.A.
    Mol. Microbiol. 70:323-340(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC1061 and K12 / MC4100.

Entry informationi

Entry nameiWZB_ECOLI
AccessioniPrimary (citable) accession number: P0AAB2
Secondary accession number(s): P77153, Q2MAY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: June 24, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.