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Protein

Chemotaxis protein CheY

Gene

cheY

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

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. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.1 Publication

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12Magnesium1 Publication1
Metal bindingi13Magnesium1
Metal bindingi57Magnesium1 Publication1
Metal bindingi59Magnesium; via carbonyl oxygen1 Publication1

GO - Molecular functioni

  • acetyltransferase activity Source: CACAO
  • magnesium ion binding Source: EcoCyc

GO - Biological processi

Keywordsi

Biological processChemotaxis, Flagellar rotation, Two-component regulatory system
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:CHEY-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheY
Gene namesi
Name:cheY
Ordered Locus Names:b1882, JW1871
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10150 cheY

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12D → A: Abolishes magnesium binding. 1 Publication1
Mutagenesisi13D → A: No effect on magnesium binding. 1 Publication1
Mutagenesisi57D → A: Abolishes magnesium binding. 1 Publication1
Mutagenesisi87T → I: Impairs chemotaxis; when associated with W-106. 1
Mutagenesisi92K → R: No effect on chemotaxis. 1 Publication1
Mutagenesisi95I → A or V: Enhanced CW flagellar rotational signaling activity. 1
Mutagenesisi95I → D, K or M: Loss of CW flagellar rotational signaling activity. 1
Mutagenesisi106Y → W: Impairs chemotaxis; when associated with I-87. 1

Chemistry databases

DrugBankiDB03487 3-Aminosuccinimide
DB04156 Aspartate Beryllium Trifluoride
DB02461 S-Methyl Phosphocysteine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000810402 – 129Chemotaxis protein CheYAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei574-aspartylphosphatePROSITE-ProRule annotation2 Publications1
Modified residuei92N6-acetyllysine2 Publications1
Modified residuei109N6-acetyllysine2 Publications1

Post-translational modificationi

Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available. The major acetylation site seems to be Lys-92. Dephosphorylated (inactivated) by CheZ.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0AE67
PRIDEiP0AE67

2D gel databases

SWISS-2DPAGEiP0AE67

PTM databases

iPTMnetiP0AE67

Interactioni

Subunit structurei

Interacts (phosphorylated CheY) with CheZ (via C-terminus).2 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi4259553, 314 interactors
ComplexPortaliCPX-1077 Chemotaxis phosphorelay complex CheA-CheY
CPX-1082 Flagellar Motor Switch Complex, CW variant
CPX-1088 Chemotaxis phosphorelay complex CheY-CheZ
DIPiDIP-6052N
IntActiP0AE67, 13 interactors
STRINGi316385.ECDH10B_2023

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0AE67
SMRiP0AE67
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AE67

Family & Domainsi

Domains and Repeats

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

Phylogenomic databases

eggNOGiENOG4108VYJ Bacteria
COG0784 LUCA
HOGENOMiHOG000034820
InParanoidiP0AE67
KOiK03413
OMAiPFQAPKV
PhylomeDBiP0AE67

Family and domain databases

CDDicd00156 REC, 1 hit
InterProiView protein in InterPro
IPR011006 CheY-like_superfamily
IPR001789 Sig_transdc_resp-reg_receiver
PfamiView protein in Pfam
PF00072 Response_reg, 1 hit
SMARTiView protein in SMART
SM00448 REC, 1 hit
SUPFAMiSSF52172 SSF52172, 1 hit
PROSITEiView protein in PROSITE
PS50110 RESPONSE_REGULATORY, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0AE67-1 [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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113A → P in AAA23570 (PubMed:3510184).Curated1

Mass spectrometryi

Molecular mass is 13966 Da from positions 2 - 129. Determined by ESI. 1 Publication
Molecular mass is 14008 Da from positions 2 - 129. Determined by ESI. With N6-acetyl-Lys-92.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02175 Genomic DNA Translation: AAA23577.1
M13463 Genomic DNA Translation: AAA23570.1
U00096 Genomic DNA Translation: AAC74952.1
AP009048 Genomic DNA Translation: BAA15698.1
PIRiE25195 QRECCY
RefSeqiNP_416396.1, NC_000913.3
WP_000763867.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74952; AAC74952; b1882
BAA15698; BAA15698; BAA15698
GeneIDi946393
KEGGiecj:JW1871
eco:b1882
PATRICifig|1411691.4.peg.365

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02175 Genomic DNA Translation: AAA23577.1
M13463 Genomic DNA Translation: AAA23570.1
U00096 Genomic DNA Translation: AAC74952.1
AP009048 Genomic DNA Translation: BAA15698.1
PIRiE25195 QRECCY
RefSeqiNP_416396.1, NC_000913.3
WP_000763867.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A0OX-ray2.95A/C/E/G2-129[»]
1AB5X-ray2.40A/B5-129[»]
1AB6X-ray2.20A/B5-129[»]
1BDJX-ray2.68A2-129[»]
1C4WX-ray1.84A2-129[»]
1CEYNMR-A2-129[»]
1CHNX-ray1.76A2-129[»]
1CYENMR-A3-129[»]
1D4ZX-ray1.90A2-129[»]
1DJMNMR-A1-129[»]
1E6KX-ray2.00A3-129[»]
1E6LX-ray1.90A3-129[»]
1E6MX-ray1.70A3-129[»]
1EAYX-ray2.00A/B2-129[»]
1EHCX-ray2.26A2-129[»]
1F4VX-ray2.22A/B/C2-129[»]
1FFGX-ray2.10A/C2-129[»]
1FFSX-ray2.40A/C2-129[»]
1FFWX-ray2.70A/C2-129[»]
1FQWX-ray2.37A/B2-129[»]
1HEYX-ray2.24A2-129[»]
1JBEX-ray1.08A2-129[»]
1KMIX-ray2.90Y1-129[»]
1MIHX-ray2.70A/B1-129[»]
1U8TX-ray1.50A/B/C/D2-129[»]
1UDRX-ray1.90A/B/C/D1-129[»]
1VLZX-ray2.05A/B2-129[»]
1YMUX-ray2.30A/B3-129[»]
1YMVX-ray1.90A3-129[»]
1ZDMX-ray2.40A/B1-129[»]
2B1JX-ray2.40A/B2-129[»]
2ID7X-ray1.75A2-129[»]
2ID9X-ray1.75A2-129[»]
2IDMX-ray2.00A2-129[»]
2LP4NMR-Y2-129[»]
3CHYX-ray1.66A2-129[»]
3F7NX-ray2.00A/B2-129[»]
3FFTX-ray2.21A/B2-129[»]
3FFWX-ray2.00A/B2-129[»]
3FFXX-ray2.01A/B2-129[»]
3FGZX-ray2.00A/B2-129[»]
3MYYX-ray2.10A/B2-129[»]
3OLVX-ray1.70A/B1-129[»]
3OLWX-ray2.30A/B1-129[»]
3OLXX-ray2.10A/B1-129[»]
3OLYX-ray2.05A/B1-129[»]
3OO0X-ray1.55A/B1-129[»]
3OO1X-ray1.70A/B1-129[»]
3RVJX-ray2.10A/B1-129[»]
3RVKX-ray1.16A1-129[»]
3RVLX-ray1.55A/B1-129[»]
3RVMX-ray1.45A1-129[»]
3RVNX-ray2.25A/B1-129[»]
3RVOX-ray1.55A1-129[»]
3RVPX-ray2.40A/B1-129[»]
3RVQX-ray1.15A1-129[»]
3RVRX-ray2.10A/B1-129[»]
3RVSX-ray2.10A/B1-129[»]
5CHYX-ray2.00A2-129[»]
5D2CX-ray2.06A/B2-129[»]
5DGCX-ray1.94A/B2-129[»]
5DKFX-ray1.94A/B2-129[»]
6CHYX-ray2.33A/B2-129[»]
ProteinModelPortaliP0AE67
SMRiP0AE67
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259553, 314 interactors
ComplexPortaliCPX-1077 Chemotaxis phosphorelay complex CheA-CheY
CPX-1082 Flagellar Motor Switch Complex, CW variant
CPX-1088 Chemotaxis phosphorelay complex CheY-CheZ
DIPiDIP-6052N
IntActiP0AE67, 13 interactors
STRINGi316385.ECDH10B_2023

Chemistry databases

DrugBankiDB03487 3-Aminosuccinimide
DB04156 Aspartate Beryllium Trifluoride
DB02461 S-Methyl Phosphocysteine

PTM databases

iPTMnetiP0AE67

2D gel databases

SWISS-2DPAGEiP0AE67

Proteomic databases

PaxDbiP0AE67
PRIDEiP0AE67

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74952; AAC74952; b1882
BAA15698; BAA15698; BAA15698
GeneIDi946393
KEGGiecj:JW1871
eco:b1882
PATRICifig|1411691.4.peg.365

Organism-specific databases

EchoBASEiEB0148
EcoGeneiEG10150 cheY

Phylogenomic databases

eggNOGiENOG4108VYJ Bacteria
COG0784 LUCA
HOGENOMiHOG000034820
InParanoidiP0AE67
KOiK03413
OMAiPFQAPKV
PhylomeDBiP0AE67

Enzyme and pathway databases

BioCyciEcoCyc:CHEY-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AE67
PROiPR:P0AE67

Family and domain databases

CDDicd00156 REC, 1 hit
InterProiView protein in InterPro
IPR011006 CheY-like_superfamily
IPR001789 Sig_transdc_resp-reg_receiver
PfamiView protein in Pfam
PF00072 Response_reg, 1 hit
SMARTiView protein in SMART
SM00448 REC, 1 hit
SUPFAMiSSF52172 SSF52172, 1 hit
PROSITEiView protein in PROSITE
PS50110 RESPONSE_REGULATORY, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCHEY_ECOLI
AccessioniPrimary (citable) accession number: P0AE67
Secondary accession number(s): P06143
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 121 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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Main funding by: National Institutes of Health

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