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Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation (By similarity).By similarity

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12MagnesiumBy similarity1
Metal bindingi13MagnesiumBy similarity1
Metal bindingi57MagnesiumBy similarity1
Metal bindingi59Magnesium; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Flagellar rotation, Two-component regulatory system

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciECOO157:CHEY-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheY
Gene namesi
Name:cheY
Ordered Locus Names:Z2936, ECs2592
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000810412 – 129Chemotaxis protein CheYAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei574-aspartylphosphatePROSITE-ProRule annotation1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei109N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP0AE68.

Interactioni

Protein-protein interaction databases

MINTiMINT-98475.
STRINGi155864.Z2936.

Structurei

3D structure databases

ProteinModelPortaliP0AE68.
SMRiP0AE68.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 124Response regulatoryPROSITE-ProRule annotationAdd BLAST118

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108VYJ. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
KOiK03413.
OMAiMLQSGAF.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG
60 70 80 90 100
YGFVISDWNM PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ
110 120
AGASGYVVKP FTAATLEEKL NKIFEKLGM
Length:129
Mass (Da):14,097
Last modified:January 23, 2007 - v2
Checksum:iE4B60B8A73DA14DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56872.1.
BA000007 Genomic DNA. Translation: BAB36015.1.
PIRiD85801.
H90952.
RefSeqiNP_310619.1. NC_002695.1.
WP_000763867.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG56872; AAG56872; Z2936.
BAB36015; BAB36015; BAB36015.
GeneIDi914203.
KEGGiece:Z2936.
ecs:ECs2592.
PATRICi18354562. VBIEscCol44059_2492.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56872.1.
BA000007 Genomic DNA. Translation: BAB36015.1.
PIRiD85801.
H90952.
RefSeqiNP_310619.1. NC_002695.1.
WP_000763867.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliP0AE68.
SMRiP0AE68.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-98475.
STRINGi155864.Z2936.

Proteomic databases

PRIDEiP0AE68.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG56872; AAG56872; Z2936.
BAB36015; BAB36015; BAB36015.
GeneIDi914203.
KEGGiece:Z2936.
ecs:ECs2592.
PATRICi18354562. VBIEscCol44059_2492.

Phylogenomic databases

eggNOGiENOG4108VYJ. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
KOiK03413.
OMAiMLQSGAF.

Enzyme and pathway databases

BioCyciECOO157:CHEY-MONOMER.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHEY_ECO57
AccessioniPrimary (citable) accession number: P0AE68
Secondary accession number(s): P06143
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.