CheY

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  • Description: two-component response regulator, modulation of flagellar switch bias

Gene name cheY
Synonyms cheB
Essential no
Product two-component response regulator
Function modulation of flagellar switch bias
Interactions involving this protein in SubtInteract: CheY
MW, pI 13 kDa, 4.746
Gene length, protein length 360 bp, 120 aa
Immediate neighbours fliY, fliZ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CheY context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

transcription factors and their control, motility and chemotaxis, phosphoproteins

This gene is a member of the following regulons

CodY regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16330

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated by CheA on an Asp residue
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:
    • in minimal medium, CheY is present with 7,100 +/- 1,000 molecules per cell PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Gerald L Hazelbauer, Wing-Cheung Lai
Bacterial chemoreceptors: providing enhanced features to two-component signaling.
Curr Opin Microbiol: 2010, 13(2);124-32
[PubMed:20122866] [WorldCat.org] [DOI] (I p)

Christopher V Rao, George W Ordal
The molecular basis of excitation and adaptation during chemotactic sensory transduction in bacteria.
Contrib Microbiol: 2009, 16;33-64
[PubMed:19494578] [WorldCat.org] [DOI] (P p)

Christopher V Rao, John R Kirby, Adam P Arkin
Phosphatase localization in bacterial chemotaxis: divergent mechanisms, convergent principles.
Phys Biol: 2005, 2(3);148-58
[PubMed:16224120] [WorldCat.org] [DOI] (I e)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)


Original Publications

Vincent J Cannistraro, George D Glekas, Christopher V Rao, George W Ordal
Cellular stoichiometry of the chemotaxis proteins in Bacillus subtilis.
J Bacteriol: 2011, 193(13);3220-7
[PubMed:21515776] [WorldCat.org] [DOI] (I p)

Y Pazy, M A Motaleb, M T Guarnieri, N W Charon, R Zhao, R E Silversmith
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.
Proc Natl Acad Sci U S A: 2010, 107(5);1924-9
[PubMed:20080618] [WorldCat.org] [DOI] (I p)

Travis J Muff, George W Ordal
The CheC phosphatase regulates chemotactic adaptation through CheD.
J Biol Chem: 2007, 282(47);34120-8
[PubMed:17908686] [WorldCat.org] [DOI] (P p)

Kazuo Kobayashi
Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2007, 66(2);395-409
[PubMed:17850253] [WorldCat.org] [DOI] (P p)

Travis J Muff, Richard M Foster, Peter J Y Liu, George W Ordal
CheX in the three-phosphatase system of bacterial chemotaxis.
J Bacteriol: 2007, 189(19);7007-13
[PubMed:17675386] [WorldCat.org] [DOI] (P p)

H Werhane, P Lopez, M Mendel, M Zimmer, G W Ordal, L M Márquez-Magaña
The last gene of the fla/che operon in Bacillus subtilis, ylxL, is required for maximal sigmaD function.
J Bacteriol: 2004, 186(12);4025-9
[PubMed:15175317] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Travis J Muff, George W Ordal
Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade.
J Biol Chem: 2004, 279(21);21787-92
[PubMed:14749334] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Michael W Bunn, Vincent J Cannistraro, George W Ordal
Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch.
J Biol Chem: 2003, 278(49);48611-6
[PubMed:12920116] [WorldCat.org] [DOI] (P p)

J R Kirby, M M Saulmon, C J Kristich, G W Ordal
CheY-dependent methylation of the asparagine receptor, McpB, during chemotaxis in Bacillus subtilis.
J Biol Chem: 1999, 274(16);11092-100
[PubMed:10196193] [WorldCat.org] [DOI] (P p)

W Estacio, S S Anna-Arriola, M Adedipe, L M Márquez-Magaña
Dual promoters are responsible for transcription initiation of the fla/che operon in Bacillus subtilis.
J Bacteriol: 1998, 180(14);3548-55
[PubMed:9657996] [WorldCat.org] [DOI] (P p)

J R Kirby, C J Kristich, S L Feinberg, G W Ordal
Methanol production during chemotaxis to amino acids in Bacillus subtilis.
Mol Microbiol: 1997, 24(4);869-78
[PubMed:9194713] [WorldCat.org] [DOI] (P p)

L M Márquez-Magaña, M J Chamberlin
Characterization of the sigD transcription unit of Bacillus subtilis.
J Bacteriol: 1994, 176(8);2427-34
[PubMed:8157612] [WorldCat.org] [DOI] (P p)

D S Bischoff, R B Bourret, M L Kirsch, G W Ordal
Purification and characterization of Bacillus subtilis CheY.
Biochemistry: 1993, 32(35);9256-61
[PubMed:8369293] [WorldCat.org] [DOI] (P p)

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