Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tyrosine-protein kinase wzc

Gene

wzc

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

Functioni

Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium. Phosphorylates udg.

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulationi

Dephosphorylated and activated by wzb.

Pathwayi: 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.

GO - Molecular functioni

  • ATPase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • protein tyrosine kinase activity Source: EcoCyc

GO - Biological processi

  • colanic acid biosynthetic process Source: EcoCyc
  • extracellular polysaccharide biosynthetic process Source: InterPro
  • lipopolysaccharide biosynthetic process Source: InterPro
  • peptidyl-tyrosine autophosphorylation Source: EcoCyc
  • peptidyl-tyrosine phosphorylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Exopolysaccharide synthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7105-MONOMER.
ECOL316407:JW2045-MONOMER.
BRENDAi2.7.10.1. 2026.
UniPathwayiUPA00631.

Protein family/group databases

TCDBi8.A.3.3.2. the cytoplasmic membrane-periplasmic auxiliary-1 (mpa1) protein with cytoplasmic (c) domain (mpa1-c or mpa1+c) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase wzc (EC:2.7.10.-)
Gene namesi
Name:wzc
Ordered Locus Names:b2060, JW2045
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13568. wzc.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131CytoplasmicSequence analysisAdd
BLAST
Transmembranei32 – 5221HelicalSequence analysisAdd
BLAST
Topological domaini53 – 424372PeriplasmicSequence analysisAdd
BLAST
Transmembranei425 – 44521HelicalSequence analysisAdd
BLAST
Topological domaini446 – 720275CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi467 – 4671Y → F: No loss of autophosphorylation. 1 Publication
Mutagenesisi491 – 4911Y → F: No loss of autophosphorylation. 1 Publication
Mutagenesisi540 – 5401K → M: Loss of autophosphorylation. 1 Publication
Mutagenesisi569 – 5691Y → F: Loss of autophosphorylation. 1 Publication
Mutagenesisi636 – 6361Y → F: No loss of autophosphorylation. 1 Publication
Mutagenesisi668 – 6681Y → F: No loss of autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Tyrosine-protein kinase wzcPRO_0000212353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei569 – 5691Phosphotyrosine; by autocatalysis1 Publication
Modified residuei708 – 7081Phosphotyrosine1 Publication
Modified residuei710 – 7101Phosphotyrosine1 Publication
Modified residuei711 – 7111Phosphotyrosine1 Publication
Modified residuei713 – 7131Phosphotyrosine1 Publication
Modified residuei715 – 7151Phosphotyrosine1 Publication

Post-translational modificationi

Autophosphorylated. Seems to be phosphorylated through a cooperative two-step mechanism. First, Tyr-569 is phosphorylated in an intramolecular reaction that generates a significant increase of protein kinase activity. Then Tyr-708, Tyr-710, Tyr-711, Tyr-713 and Tyr-715 are phosphorylated in an intermolecular Tyr-569-dependent reaction.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP76387.
PaxDbiP76387.
PRIDEiP76387.

PTM databases

iPTMnetiP76387.

Interactioni

Protein-protein interaction databases

BioGridi4262960. 334 interactions.
DIPiDIP-28075N.
IntActiP76387. 4 interactions.
MINTiMINT-8293229.
STRINGi511145.b2060.

Structurei

Secondary structure

1
720
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi456 – 4605Combined sources
Turni461 – 4633Combined sources
Beta strandi466 – 4716Combined sources
Helixi474 – 4785Combined sources
Helixi497 – 5004Combined sources
Helixi505 – 52016Combined sources
Turni522 – 5254Combined sources
Beta strandi528 – 53912Combined sources
Helixi540 – 55213Combined sources
Turni553 – 5553Combined sources
Beta strandi558 – 5625Combined sources
Turni565 – 5673Combined sources
Helixi570 – 5745Combined sources
Helixi582 – 5876Combined sources
Turni592 – 5954Combined sources
Beta strandi604 – 6074Combined sources
Helixi616 – 6205Combined sources
Helixi623 – 63513Combined sources
Beta strandi637 – 6426Combined sources
Turni646 – 6483Combined sources
Helixi651 – 6555Combined sources
Turni656 – 6583Combined sources
Beta strandi660 – 6678Combined sources
Turni668 – 6703Combined sources
Helixi673 – 68513Combined sources
Beta strandi692 – 6987Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LA6X-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P447-720[»]
ProteinModelPortaliP76387.
SMRiP76387. Positions 450-718.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the etk/wzc family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D75. Bacteria.
COG0489. LUCA.
COG3206. LUCA.
HOGENOMiHOG000153997.
InParanoidiP76387.
KOiK16692.
OMAiTKDHPAY.
OrthoDBiEOG69D3H6.
PhylomeDBiP76387.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR025669. AAA_dom.
IPR005702. EPS_synthesis.
IPR032807. GNVR.
IPR003856. LipoPS_biosynth.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF13614. AAA_31. 1 hit.
PF13807. GNVR. 1 hit.
PF02706. Wzz. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01007. eps_fam. 1 hit.

Sequencei

Sequence statusi: Complete.

P76387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEKVKQHAA PVTGSDEIDI GRLVGTVIEA RWWVIGITTV FALCAVVYTF
60 70 80 90 100
FATPIYSADA LVQIEQNSGN SLVQDIGSAL ANKPPASDAE IQLIRSRLVL
110 120 130 140 150
GKTVDDLDLD IAVSKNTFPI FGAGWDRLMG RQNETVKVTT FNRPKEMADQ
160 170 180 190 200
VFTLNVLDNK NYTLSSDGGF SARGQAGQML KKEGVTLMVE AIHASPGSEF
210 220 230 240 250
TVTKYSTLGM INQLQNSLTV TENGKDAGVL SLTYTGEDRE QIRDILNSIA
260 270 280 290 300
RNYQEQNIER KSAEASKSLA FLAQQLPEVR SRLDVAENKL NAFRQDKDSV
310 320 330 340 350
DLPLEAKAVL DSMVNIDAQL NELTFKEAEI SKLYTKVHPA YRTLLEKRQA
360 370 380 390 400
LEDEKAKLNG RVTAMPKTQQ EIVRLTRDVE SGQQVYMQLL NKEQELKITE
410 420 430 440 450
ASTVGDVRIV DPAITQPGVL KPKKGLIILG AIILGLMLSI VGVLLRSLFN
460 470 480 490 500
RGIESPQVLE EHGISVYASI PLSEWQKARD SVKTIKGIKR YKQSQLLAVG
510 520 530 540 550
NPTDLAIEAI RSLRTSLHFA MMQAQNNVLM MTGVSPSIGK TFVCANLAAV
560 570 580 590 600
ISQTNKRVLL IDCDMRKGYT HELLGTNNVN GLSEILIGQG DITTAAKPTS
610 620 630 640 650
IAKFDLIPRG QVPPNPSELL MSERFAELVN WASKNYDLVL IDTPPILAVT
660 670 680 690 700
DAAIVGRHVG TTLMVARYAV NTLKEVETSL SRFEQNGIPV KGVILNSIFR
710 720
RASAYQDYGY YEYEYKSDAK
Length:720
Mass (Da):79,343
Last modified:April 3, 2002 - v2
Checksum:i8F61017B5ECFFB45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38473 Genomic DNA. Translation: AAC77835.1.
U00096 Genomic DNA. Translation: AAC75121.2.
AP009048 Genomic DNA. Translation: BAA15913.1.
PIRiC64972.
RefSeqiNP_416564.4. NC_000913.3.
WP_000137196.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75121; AAC75121; b2060.
BAA15913; BAA15913; BAA15913.
GeneIDi946567.
KEGGiecj:JW2045.
eco:b2060.
PATRICi32119453. VBIEscCol129921_2137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38473 Genomic DNA. Translation: AAC77835.1.
U00096 Genomic DNA. Translation: AAC75121.2.
AP009048 Genomic DNA. Translation: BAA15913.1.
PIRiC64972.
RefSeqiNP_416564.4. NC_000913.3.
WP_000137196.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LA6X-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P447-720[»]
ProteinModelPortaliP76387.
SMRiP76387. Positions 450-718.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262960. 334 interactions.
DIPiDIP-28075N.
IntActiP76387. 4 interactions.
MINTiMINT-8293229.
STRINGi511145.b2060.

Protein family/group databases

TCDBi8.A.3.3.2. the cytoplasmic membrane-periplasmic auxiliary-1 (mpa1) protein with cytoplasmic (c) domain (mpa1-c or mpa1+c) family.

PTM databases

iPTMnetiP76387.

Proteomic databases

EPDiP76387.
PaxDbiP76387.
PRIDEiP76387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75121; AAC75121; b2060.
BAA15913; BAA15913; BAA15913.
GeneIDi946567.
KEGGiecj:JW2045.
eco:b2060.
PATRICi32119453. VBIEscCol129921_2137.

Organism-specific databases

EchoBASEiEB3338.
EcoGeneiEG13568. wzc.

Phylogenomic databases

eggNOGiENOG4105D75. Bacteria.
COG0489. LUCA.
COG3206. LUCA.
HOGENOMiHOG000153997.
InParanoidiP76387.
KOiK16692.
OMAiTKDHPAY.
OrthoDBiEOG69D3H6.
PhylomeDBiP76387.

Enzyme and pathway databases

UniPathwayiUPA00631.
BioCyciEcoCyc:G7105-MONOMER.
ECOL316407:JW2045-MONOMER.
BRENDAi2.7.10.1. 2026.

Miscellaneous databases

PROiP76387.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR025669. AAA_dom.
IPR005702. EPS_synthesis.
IPR032807. GNVR.
IPR003856. LipoPS_biosynth.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF13614. AAA_31. 1 hit.
PF13807. GNVR. 1 hit.
PF02706. Wzz. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01007. eps_fam. 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 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "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: CHARACTERIZATION.
    Strain: K12 / JM109 / ATCC 53323.
  6. "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: CHARACTERIZATION.
    Strain: K12 / JM109 / ATCC 53323.
  7. "Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process."
    Grangeasse C., Doublet P., Cozzone A.J.
    J. Biol. Chem. 277:7127-7135(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS.
    Strain: K12 / JM109 / ATCC 53323.
  8. "Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase."
    Grangeasse C., Obadia B., Mijakovic I., Deutscher J., Cozzone A.J., Doublet P.
    J. Biol. Chem. 278:39323-39329(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF UDG.
  9. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiWZC_ECOLI
AccessioniPrimary (citable) accession number: P76387
Secondary accession number(s): O08003, O08004, P71236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: April 3, 2002
Last modified: April 13, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Additional site-directed mutagenesis experiments indicated that the tyrosine residues at positions 708, 710, 711, 713 and 715 are phosphorylation sites, whereas tyrosine at position 705 is not.

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

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 one 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.