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P0AE67

- CHEY_ECOLI

UniProt

P0AE67 - CHEY_ECOLI

Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    Binds 1 magnesium 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

    1. acetyltransferase activity Source: CACAO
    2. magnesium ion binding Source: EcoCyc
    3. phosphorelay response regulator activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. bacterial-type flagellum-dependent cell motility Source: EcoCyc
    2. chemotaxis Source: EcoCyc
    3. internal peptidyl-lysine acetylation Source: CACAO
    4. phosphorelay signal transduction system Source: EcoCyc
    5. protein acetylation Source: EcoCyc

    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
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10150. cheY.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 methioninei1 – 11Removed
    Chaini2 – 129128Chemotaxis protein CheYPRO_0000081040Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 5714-aspartylphosphate3 PublicationsPROSITE-ProRule annotation
    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AE67.

    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

    DIPiDIP-48237N.
    IntActiP0AE67. 12 interactions.
    STRINGi511145.b1882.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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

    eggNOGiCOG0784.
    HOGENOMiHOG000034820.
    KOiK03413.
    OMAiGSCARIR.
    OrthoDBiEOG6PKFC7.
    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

    MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG    50
    YGFVISDWNM PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ 100
    AGASGYVVKP FTAATLEEKL NKIFEKLGM 129
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490144.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74952; AAC74952; b1882.
    BAA15698; BAA15698; BAA15698.
    GeneIDi12930559.
    946393.
    KEGGiecj:Y75_p1858.
    eco:b1882.
    PATRICi32119091. VBIEscCol129921_1963.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi E25195. QRECCY.
    RefSeqi NP_416396.1. NC_000913.3.
    YP_490144.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A0O X-ray 2.95 A/C/E/G 2-129 [» ]
    1AB5 X-ray 2.40 A/B 5-129 [» ]
    1AB6 X-ray 2.20 A/B 5-129 [» ]
    1BDJ X-ray 2.68 A 2-129 [» ]
    1C4W X-ray 1.84 A 2-129 [» ]
    1CEY NMR - A 2-129 [» ]
    1CHN X-ray 1.76 A 2-129 [» ]
    1CYE NMR - A 3-129 [» ]
    1D4Z X-ray 1.90 A 2-129 [» ]
    1DJM NMR - A 1-129 [» ]
    1E6K X-ray 2.00 A 3-129 [» ]
    1E6L X-ray 1.90 A 3-129 [» ]
    1E6M X-ray 1.70 A 3-129 [» ]
    1EAY X-ray 2.00 A/B 2-129 [» ]
    1EHC X-ray 2.26 A 2-129 [» ]
    1F4V X-ray 2.22 A/B/C 2-129 [» ]
    1FFG X-ray 2.10 A/C 2-129 [» ]
    1FFS X-ray 2.40 A/C 2-129 [» ]
    1FFW X-ray 2.70 A/C 2-129 [» ]
    1FQW X-ray 2.37 A/B 2-129 [» ]
    1HEY X-ray 2.24 A 2-129 [» ]
    1JBE X-ray 1.08 A 2-129 [» ]
    1KMI X-ray 2.90 Y 1-129 [» ]
    1MIH X-ray 2.70 A/B 1-129 [» ]
    1U8T X-ray 1.50 A/B/C/D 2-129 [» ]
    1UDR X-ray 1.90 A/B/C/D 1-129 [» ]
    1VLZ X-ray 2.05 A/B 2-129 [» ]
    1YMU X-ray 2.30 A/B 3-129 [» ]
    1YMV X-ray 1.90 A 3-129 [» ]
    1ZDM X-ray 2.40 A/B 1-129 [» ]
    2B1J X-ray 2.40 A/B 2-129 [» ]
    2ID7 X-ray 1.75 A 2-129 [» ]
    2ID9 X-ray 1.75 A 2-129 [» ]
    2IDM X-ray 2.00 A 2-129 [» ]
    2LP4 NMR - Y 2-129 [» ]
    3CHY X-ray 1.66 A 2-129 [» ]
    3F7N X-ray 2.00 A/B 2-129 [» ]
    3FFT X-ray 2.21 A/B 2-129 [» ]
    3FFW X-ray 2.00 A/B 2-129 [» ]
    3FFX X-ray 2.01 A/B 2-129 [» ]
    3FGZ X-ray 2.00 A/B 2-129 [» ]
    3MYY X-ray 2.10 A/B 2-129 [» ]
    3OLV X-ray 1.70 A/B 1-129 [» ]
    3OLW X-ray 2.30 A/B 1-129 [» ]
    3OLX X-ray 2.10 A/B 1-129 [» ]
    3OLY X-ray 2.05 A/B 1-129 [» ]
    3OO0 X-ray 1.55 A/B 1-129 [» ]
    3OO1 X-ray 1.70 A/B 1-129 [» ]
    3RVJ X-ray 2.10 A/B 1-129 [» ]
    3RVK X-ray 1.16 A 1-129 [» ]
    3RVL X-ray 1.55 A/B 1-129 [» ]
    3RVM X-ray 1.45 A 1-129 [» ]
    3RVN X-ray 2.25 A/B 1-129 [» ]
    3RVO X-ray 1.55 A 1-129 [» ]
    3RVP X-ray 2.40 A/B 1-129 [» ]
    3RVQ X-ray 1.15 A 1-129 [» ]
    3RVR X-ray 2.10 A/B 1-129 [» ]
    3RVS X-ray 2.10 A/B 1-129 [» ]
    5CHY X-ray 2.00 A 2-129 [» ]
    6CHY X-ray 2.33 A/B 2-129 [» ]
    ProteinModelPortali P0AE67.
    SMRi P0AE67. Positions 2-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48237N.
    IntActi P0AE67. 12 interactions.
    STRINGi 511145.b1882.

    2D gel databases

    SWISS-2DPAGE P0AE67.

    Proteomic databases

    PaxDbi P0AE67.
    PRIDEi P0AE67.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74952 ; AAC74952 ; b1882 .
    BAA15698 ; BAA15698 ; BAA15698 .
    GeneIDi 12930559.
    946393.
    KEGGi ecj:Y75_p1858.
    eco:b1882.
    PATRICi 32119091. VBIEscCol129921_1963.

    Organism-specific databases

    EchoBASEi EB0148.
    EcoGenei EG10150. cheY.

    Phylogenomic databases

    eggNOGi COG0784.
    HOGENOMi HOG000034820.
    KOi K03413.
    OMAi GSCARIR.
    OrthoDBi EOG6PKFC7.
    PhylomeDBi P0AE67.

    Enzyme and pathway databases

    BioCyci EcoCyc:CHEY-MONOMER.
    ECOL316407:JW1871-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AE67.
    PROi P0AE67.

    Gene expression databases

    Genevestigatori P0AE67.

    Family and domain databases

    InterProi IPR011006. CheY-like_superfamily.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view ]
    Pfami PF00072. Response_reg. 1 hit.
    [Graphical view ]
    SMARTi SM00448. REC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52172. SSF52172. 1 hit.
    PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. 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. Cited for: STRUCTURE BY NMR.

    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: October 1, 2014
    This is version 94 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

    External Data

    Dasty 3