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Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Magnesium1 Publication
Metal bindingi13 – 131Magnesium
Metal bindingi57 – 571Magnesium1 Publication
Metal bindingi59 – 591Magnesium; via carbonyl oxygen1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • bacterial-type flagellum-dependent cell motility Source: EcoCyc
  • chemotaxis Source: EcoCyc
  • internal peptidyl-lysine acetylation Source: CACAO
  • phosphorelay signal transduction system Source: EcoCyc
  • protein acetylation Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Flagellar rotation, Two-component regulatory system

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:CHEY-MONOMER.
ECOL316407:JW1871-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10150. cheY.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121D → A: Abolishes magnesium binding. 1 Publication
Mutagenesisi13 – 131D → A: No effect on magnesium binding. 1 Publication
Mutagenesisi57 – 571D → A: Abolishes magnesium binding. 1 Publication
Mutagenesisi87 – 871T → I: Impairs chemotaxis; when associated with W-106.
Mutagenesisi92 – 921K → R: No effect on chemotaxis. 1 Publication
Mutagenesisi95 – 951I → A or V: Enhanced CW flagellar rotational signaling activity.
Mutagenesisi95 – 951I → D, K or M: Loss of CW flagellar rotational signaling activity.
Mutagenesisi106 – 1061Y → W: Impairs chemotaxis; when associated with I-87.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 129128Chemotaxis protein CheYPRO_0000081040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 5714-aspartylphosphatePROSITE-ProRule annotation2 Publications
Modified residuei92 – 921N6-acetyllysine1 Publication
Modified residuei109 – 1091N6-acetyllysine2 Publications

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.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0AE67.
PRIDEiP0AE67.

2D gel databases

SWISS-2DPAGEP0AE67.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
cheAP073633EBI-546693,EBI-1026773
cheZP0A9H93EBI-546693,EBI-546726

Protein-protein interaction databases

BioGridi4259553. 304 interactions.
DIPiDIP-6052N.
IntActiP0AE67. 12 interactions.
STRINGi511145.b1882.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi8 – 114Combined sources
Helixi15 – 2713Combined sources
Beta strandi33 – 386Combined sources
Helixi39 – 468Combined sources
Turni47 – 493Combined sources
Beta strandi53 – 586Combined sources
Beta strandi61 – 633Combined sources
Helixi65 – 739Combined sources
Turni76 – 805Combined sources
Beta strandi83 – 897Combined sources
Helixi92 – 1009Combined sources
Beta strandi104 – 1107Combined sources
Helixi113 – 12715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AE67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 124118Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108VYJ. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
InParanoidiP0AE67.
KOiK03413.
OMAiMLQSGAF.
PhylomeDBiP0AE67.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131A → P in AAA23570 (PubMed:3510184).Curated

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.
PATRICi32119091. VBIEscCol129921_1963.

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
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. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259553. 304 interactions.
DIPiDIP-6052N.
IntActiP0AE67. 12 interactions.
STRINGi511145.b1882.

2D gel databases

SWISS-2DPAGEP0AE67.

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.
PATRICi32119091. VBIEscCol129921_1963.

Organism-specific databases

EchoBASEiEB0148.
EcoGeneiEG10150. cheY.

Phylogenomic databases

eggNOGiENOG4108VYJ. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
InParanoidiP0AE67.
KOiK03413.
OMAiMLQSGAF.
PhylomeDBiP0AE67.

Enzyme and pathway databases

BioCyciEcoCyc:CHEY-MONOMER.
ECOL316407:JW1871-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AE67.
PROiP0AE67.

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_ECOLI
AccessioniPrimary (citable) accession number: P0AE67
Secondary accession number(s): P06143
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 108 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

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.