P71403 · CHEY1_HELPY

Function

function

Chemotactic response regulator protein that modulates the rotation direction of bacterial flagellar motors. Plays an important role in the colonization and infection of Helicobacter pylori (PubMed:10722597).
Upon phosphorylation by CheA, interacts with the flagellar motor protein FliM to cause clockwise flagellar rotation and bacterial reversals, as opposed to straight swimming when CheY1 is not phosphorylated (PubMed:20207758).

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site.

1124102030405060708090100110120
TypeIDPosition(s)Description
Binding site7Mg2+ (UniProtKB | ChEBI)
Binding site8Mg2+ (UniProtKB | ChEBI)
Binding site53Mg2+ (UniProtKB | ChEBI)
Binding site55Mg2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Biological Processarchaeal or bacterial-type flagellum-dependent cell motility
Biological Processchemotaxis
Biological Processphosphorelay signal transduction system

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chemotaxis protein CheY1

Gene names

    • Name
      cheY1
    • Ordered locus names
      HP_1067

Organism names

Accessions

  • Primary accession
    P71403
  • Secondary accessions
    • O07677

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant122in strain: NCTC 11637 and NCTC 11638

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000810501-124Chemotaxis protein CheY1
Modified residue534-aspartylphosphate

Post-translational modification

Phosphorylated by CheAY (PubMed:16207913).
Dephosphorylated (inactivated) by CheZ (PubMed:16207913, PubMed:20497335).

Keywords

Proteomic databases

Interaction

Subunit

Interacts (when phosphorylated) with FliM.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P71403cheAY O251533EBI-6409045, EBI-6410665

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-120Response regulatory

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    124
  • Mass (Da)
    13,915
  • Last updated
    1997-11-01 v2
  • Checksum
    F2B40BC0C04FCBFA
MKLLVVDDSSTMRRIIKNTLSRLGYEDVLEAEHGVEAWEKLDANADTKVLITDWNMPEMNGLDLVKKVRSDSRFKEIPIIMITTEGGKAEVITALKAGVNNYIVKPFTPQVLKEKLEVVLGTND

Sequence caution

The sequence CAA57487.1 differs from that shown. Reason: Erroneous initiation

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X81897
EMBL· GenBank· DDBJ
CAA57487.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
U97567
EMBL· GenBank· DDBJ
AAB66375.1
EMBL· GenBank· DDBJ
Genomic DNA
AE000511
EMBL· GenBank· DDBJ
AAD08113.1
EMBL· GenBank· DDBJ
Genomic DNA
AF021090
EMBL· GenBank· DDBJ
AAD01682.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp