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P0AE67 (CHEY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chemotaxis protein CheY
Gene names
Name:cheY
Ordered Locus Names:b1882, JW1871
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14

Cofactor

Binds 1 magnesium ion per subunit.

Subunit structure

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

Subcellular location

Cytoplasm.

Post-translational modification

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. Ref.6 Ref.7 Ref.9 Ref.13

Sequence similarities

Contains 1 response regulatory domain.

Mass spectrometry

Molecular mass is 13966 Da from positions 2 - 129. Determined by ESI. Ref.11

Molecular mass is 14008 Da from positions 2 - 129. Determined by ESI. With N6-acetyl-Lys-92. Ref.11

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 129128Chemotaxis protein CheY
PRO_0000081040

Regions

Domain7 – 124118Response regulatory

Sites

Metal binding121Magnesium Ref.16
Metal binding131Magnesium
Metal binding571Magnesium Ref.16
Metal binding591Magnesium; via carbonyl oxygen Ref.16

Amino acid modifications

Modified residue5714-aspartylphosphate Ref.15
Modified residue921N6-acetyllysine Ref.11 Ref.12
Modified residue1091N6-acetyllysine Ref.8 Ref.11

Experimental info

Mutagenesis121D → A: Abolishes magnesium binding. Ref.25
Mutagenesis131D → A: No effect on magnesium binding. Ref.25
Mutagenesis571D → A: Abolishes magnesium binding. Ref.25
Mutagenesis871T → I: Impairs chemotaxis; when associated with W-106.
Mutagenesis921K → R: No effect on chemotaxis. Ref.11
Mutagenesis951I → A or V: Enhanced CW flagellar rotational signaling activity.
Mutagenesis951I → D, K or M: Loss of CW flagellar rotational signaling activity.
Mutagenesis1061Y → W: Impairs chemotaxis; when associated with I-87.
Sequence conflict1131A → P in AAA23570. Ref.2

Secondary structure

........................... 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AE67 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E4B60B8A73DA14DC

FASTA12914,097
        10         20         30         40         50         60 
MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM 

        70         80         90        100        110        120 
PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL 


NKIFEKLGM 

« Hide

References

« Hide 'large scale' references
[1]"Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein."
Matsumura P., Rydel J.J., Linzmeier R., Vacante D.
J. Bacteriol. 160:36-41(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli."
Mutoh N., Simon M.I.
J. Bacteriol. 165:161-166(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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.
[6]"Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis."
Hess J.F., Oosawa K., Kaplan N., Simon M.I.
Cell 53:79-87(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[7]"Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY."
Sanders D.A., Gillece-Castro B.L., Stock A.M., Burlingame A.L., Koshland D.E. Jr.
J. Biol. Chem. 264:21770-21778(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT ASP-57, PARTIAL PROTEIN SEQUENCE.
[8]"Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch."
Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M.
Biochemistry 31:10099-10107(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-109.
[9]"Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate."
Wang H., Matsumura P.
Mol. Microbiol. 19:695-703(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION BY CHEAS/CHEZ COMPLEX.
[10]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[11]"Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY."
Ramakrishnan R., Schuster M., Bourret R.B.
Proc. Natl. Acad. Sci. U.S.A. 95:4918-4923(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-92 AND LYS-109 BY ACETYL-COA SYNTHETASE, MASS SPECTROMETRY, MUTAGENESIS OF LYS-92.
[12]"Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis."
Barak R., Eisenbach M.
Mol. Microbiol. 40:731-743(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF ACETYLATION AT LYS-92 IN CHEMOTAXIS.
[13]"Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ. Modulation of activity by the phosphorylated CheY substrate."
Silversmith R.E., Levin M.D., Schilling E., Bourret R.B.
J. Biol. Chem. 283:756-765(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION BY CHEZ.
[14]"The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."
Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.
Mol. Cell 38:128-139(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: K12 / RP3098.
[15]"Crystal structure of Escherichia coli CheY refined at 1.7-A resolution."
Volz K., Matsumura P.
J. Biol. Chem. 266:15511-15519(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[16]"Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface."
Bellsolell L., Prieto J., Serrano L., Coll M.
J. Mol. Biol. 238:489-495(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
[17]Erratum
Bellsolell L., Prieto J., Serrano L., Coll M.
J. Mol. Biol. 242:103-103(1994)
[18]"The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism."
Bellsolell L., Cronet P., Majolero M., Serrano L., Coll M.
J. Mol. Biol. 257:116-128(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS GLY-17 AND GLY-14/GLY-15/GLY-17.
[19]"Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106."
Zhu X., Rebello J., Matsumura P., Volz K.
J. Biol. Chem. 272:5000-5006(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS TRP-106 AND ILE-87/TRP-106.
[20]"Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability."
Wilcock D., Pisabarro M.T., Lopez-Hernandez E., Serrano L., Coll M.
Acta Crystallogr. D 54:378-385(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[21]"Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY."
Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P.
Nat. Struct. Biol. 5:25-29(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CHEA.
[22]"Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway."
McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W.
Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[23]"Correlated switch binding and signaling in bacterial chemotaxis."
Schuster M., Zhao R., Bourret R.B., Collins E.J.
J. Biol. Chem. 275:19752-19758(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT VAL-95.
[24]"Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY."
Kato M., Mizuno T., Hakoshima T.
Acta Crystallogr. D 54:140-142(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH ARCB.
[25]"Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY."
Sola M., Lopez-Hernandez E., Cronet P., Lacroix E., Serrano L., Coll M., Parraga A.
J. Mol. Biol. 303:213-225(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MUTAGENESIS OF ASP-12; ASP-13 AND ASP-57.
[26]"Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ."
Zhao R., Collins E.J., Bourret R.B., Silversmith R.E.
Nat. Struct. Biol. 9:570-575(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CHEZ.
[27]"1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein."
Bruix M., Pascual J., Santoro J., Prieto J., Serrano L., Rico M.
Eur. J. Biochem. 215:573-585(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[28]"NMR structure of activated CheY."
Cho H.S., Lee S.-Y., Yan D., Pan X., Parkinson J.S., Kustu S., Wemmer D.E., Pelton J.G.
J. Mol. Biol. 297:543-551(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02175 Genomic DNA. Translation: AAA23577.1.
M13463 Genomic DNA. Translation: AAA23570.1.
U00096 Genomic DNA. Translation: AAC74952.1.
AP009048 Genomic DNA. Translation: BAA15698.1.
PIRQRECCY. E25195.
RefSeqNP_416396.1. NC_000913.3.
YP_490144.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D3-129[»]
1VLZX-ray2.05A/B2-129[»]
1YMUX-ray2.30A/B3-129[»]
1YMVX-ray1.90A3-129[»]
1ZDMX-ray2.40A/B1-129[»]
2B1JX-ray2.40A/B2-128[»]
2ID7X-ray1.75A2-128[»]
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[»]
6CHYX-ray2.33A/B2-129[»]
ProteinModelPortalP0AE67.
SMRP0AE67. Positions 2-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48237N.
IntActP0AE67. 12 interactions.
STRING511145.b1882.

2D gel databases

SWISS-2DPAGEP0AE67.

Proteomic databases

PaxDbP0AE67.
PRIDEP0AE67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74952; AAC74952; b1882.
BAA15698; BAA15698; BAA15698.
GeneID12930559.
946393.
KEGGecj:Y75_p1858.
eco:b1882.
PATRIC32119091. VBIEscCol129921_1963.

Organism-specific databases

EchoBASEEB0148.
EcoGeneEG10150. cheY.

Phylogenomic databases

eggNOGCOG0784.
HOGENOMHOG000034820.
KOK03413.
OMAFGFVISD.
OrthoDBEOG6PKFC7.
PhylomeDBP0AE67.
ProtClustDBPRK10610.

Enzyme and pathway databases

BioCycEcoCyc:CHEY-MONOMER.
ECOL316407:JW1871-MONOMER.

Gene expression databases

GenevestigatorP0AE67.

Family and domain databases

InterProIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52172. SSF52172. 1 hit.
PROSITEPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AE67.
PROP0AE67.

Entry information

Entry nameCHEY_ECOLI
AccessionPrimary (citable) accession number: P0AE67
Secondary accession number(s): P06143
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene