Chemotaxis protein CheY

Details

Name
Chemotaxis protein CheY
Synonyms
Not Available
Gene Name
cheY
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011458|Chemotaxis protein CheY
MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNM
PNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL
NKIFEKLGM
Number of residues
129
Molecular Weight
14097.24
Theoretical pI
4.61
GO Classification
Functions
acetyltransferase activity / magnesium ion binding
Processes
bacterial-type flagellum-dependent cell motility / chemotaxis / internal peptidyl-lysine acetylation / phosphorelay signal transduction system / protein acetylation
Components
cytosol
General Function
Magnesium ion binding
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011459|Chemotaxis protein CheY (cheY)
ATGGCGGATAAAGAACTTAAATTTTTGGTTGTGGATGACTTTTCCACCATGCGACGCATA
GTGCGTAACCTGCTGAAAGAGCTGGGATTCAATAATGTTGAGGAAGCGGAAGATGGCGTC
GACGCTCTCAATAAGTTGCAGGCAGGCGGTTATGGATTTGTTATCTCCGACTGGAACATG
CCCAATATGGATGGCCTGGAATTGCTGAAAACAATTCGTGCGGATGGCGCGATGTCGGCA
TTGCCAGTGTTAATGGTGACTGCAGAAGCGAAGAAAGAGAACATCATTGCTGCGGCGCAA
GCGGGGGCCAGTGGCTATGTGGTGAAGCCATTTACCGCCGCGACGCTGGAGGAAAAACTC
AACAAAATCTTTGAGAAACTGGGCATGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AE67
UniProtKB Entry NameCHEY_ECOLI
GenBank Protein ID7144481
GenBank Gene IDK02175
General References
  1. Matsumura P, Rydel JJ, Linzmeier R, Vacante D: Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein. J Bacteriol. 1984 Oct;160(1):36-41. [Article]
  2. Mutoh N, Simon MI: Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli. J Bacteriol. 1986 Jan;165(1):161-6. [Article]
  3. Itoh T, Aiba H, Baba T, 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, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: 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. DNA Res. 1996 Dec 31;3(6):379-92. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Hess JF, Oosawa K, Kaplan N, Simon MI: Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell. 1988 Apr 8;53(1):79-87. [Article]
  7. Sanders DA, Gillece-Castro BL, Stock AM, Burlingame AL, Koshland DE Jr: Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. J Biol Chem. 1989 Dec 25;264(36):21770-8. [Article]
  8. Barak R, Welch M, Yanovsky A, Oosawa K, Eisenbach M: Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch. Biochemistry. 1992 Oct 20;31(41):10099-107. [Article]
  9. Wang H, Matsumura P: Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate. Mol Microbiol. 1996 Feb;19(4):695-703. [Article]
  10. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  11. Ramakrishnan R, Schuster M, Bourret RB: Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY. Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4918-23. [Article]
  12. Barak R, Eisenbach M: Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis. Mol Microbiol. 2001 May;40(3):731-43. [Article]
  13. Silversmith RE, Levin MD, Schilling E, Bourret RB: Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ. Modulation of activity by the phosphorylated CheY substrate. J Biol Chem. 2008 Jan 11;283(2):756-65. Epub 2007 Nov 12. [Article]
  14. Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM: The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol Cell. 2010 Apr 9;38(1):128-39. doi: 10.1016/j.molcel.2010.03.001. Epub 2010 Mar 25. [Article]
  15. Volz K, Matsumura P: Crystal structure of Escherichia coli CheY refined at 1.7-A resolution. J Biol Chem. 1991 Aug 15;266(23):15511-9. [Article]
  16. Bellsolell L, Prieto J, Serrano L, Coll M: Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J Mol Biol. 1994 May 13;238(4):489-95. [Article]
  17. Bellsolell L, Cronet P, Majolero M, Serrano L, Coll M: The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism. J Mol Biol. 1996 Mar 22;257(1):116-28. [Article]
  18. Zhu X, Rebello J, Matsumura P, Volz K: Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106. J Biol Chem. 1997 Feb 21;272(8):5000-6. [Article]
  19. Wilcock D, Pisabarro MT, Lopez-Hernandez E, Serrano L, Coll M: Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability. Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):378-85. [Article]
  20. Welch M, Chinardet N, Mourey L, Birck C, Samama JP: Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat Struct Biol. 1998 Jan;5(1):25-9. [Article]
  21. McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW: Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. [Article]
  22. Schuster M, Zhao R, Bourret RB, Collins EJ: Correlated switch binding and signaling in bacterial chemotaxis. J Biol Chem. 2000 Jun 30;275(26):19752-8. [Article]
  23. Kato M, Mizuno T, Hakoshima T: Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY. Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):140-2. [Article]
  24. Sola M, Lopez-Hernandez E, Cronet P, Lacroix E, Serrano L, Coll M, Parraga A: Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY. J Mol Biol. 2000 Oct 20;303(2):213-25. [Article]
  25. Zhao R, Collins EJ, Bourret RB, Silversmith RE: Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Nat Struct Biol. 2002 Aug;9(8):570-5. [Article]
  26. Bruix M, Pascual J, Santoro J, Prieto J, Serrano L, Rico M: 1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein. Eur J Biochem. 1993 Aug 1;215(3):573-85. [Article]
  27. Cho HS, Lee SY, Yan D, Pan X, Parkinson JS, Kustu S, Wemmer DE, Pelton JG: NMR structure of activated CheY. J Mol Biol. 2000 Mar 31;297(3):543-51. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02461S-Methyl PhosphocysteineexperimentalunknownDetails
DB03487(S)-AspartimideexperimentalunknownDetails
DB04156Aspartate beryllium trifluorideexperimentalunknownDetails