CheY

• 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
Gene expression levels in SubtiExpress: cheY
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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, DegU regulon, SigD regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU16330

Database entries

• BsubCyc: BSU16330

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): YneI

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated by CheA on an Asp residue
  • dephosphorylated by CheC PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • CheY-P-CheC PubMed
  • CheA-CheY

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU16330

• Structure: 1TMY (CheY from Thermotoga maritima)

• UniProt: P24072

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: part of the fla-che operon
  • flgB-flgC-fliE-fliF-fliG-fliH-fliI-fliJ-ylxF-fliK-flgD-flgE-fliL-fliM-fliY-cheY-fliZ-fliP-fliQ-fliR-flhB-flhA-flhF-flhG-cheB-cheA-cheW-cheC-cheD-sigD-swrB PubMed
  • ylxF-fliK-flgD-flgE-fliL-fliM-fliY-cheY-fliZ-fliP-fliQ-fliR-flhB-flhA-flhF-flhG-cheB-cheA-cheW-cheC-cheD-sigD-swrB PubMed

• Expression browser: cheY PubMed

• Sigma factor:
  • flgB: SigA PubMed, SigD PubMed
  • ylxF: SigD PubMed

• Regulation: see fla-che operon

• Regulatory mechanism: see fla-che operon

• Additional information:
  • in minimal medium, CheY is present with 7,100 +/- 1,000 molecules per cell PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1164 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2117 PubMed

Biological materials

• Mutant:
  • 1A798 ( cheY::cat), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

Serena Mordini, Cecilia Osera, Simone Marini, Francesco Scavone, Riccardo Bellazzi, Alessandro Galizzi, Cinzia Calvio
The role of SwrA, DegU and P(D3) in fla/che expression in B. subtilis.
PLoS One: 2013, 8(12);e85065
[PubMed:24386445] [WorldCat.org] [DOI] (I e)

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)