CheA

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  • Description: two-component sensor kinase, chemotactic signal modulator

Gene name cheA
Synonyms cheN
Essential no
Product two-component sensor kinase
Function chemotactic signal modulator
Gene expression levels in SubtiExpress: cheA
Interactions involving this protein in SubtInteract: CheA
MW, pI 74 kDa, 4.452
Gene length, protein length 2013 bp, 671 aa
Immediate neighbours cheB, cheW
Sequences Protein DNA DNA_with_flanks
Genetic context
CheA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CheA expression.png















Categories containing this gene/protein

protein modification, transcription factors and their control, motility and chemotaxis, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CodY regulon, DegU regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16430

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of CheY and CheB PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity:
    • phosphorylation of CheA is stimulated by interaction with the complex of deaminated McpC-CheD PubMed
    • the kinase activity of CheA is activated by chemoreceptors bound to CheD PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Additional information:
    • in minimal medium, CheA is present with 2,600 +/- 560 molecules per cell PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 705 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1580 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 483 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 188 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 62 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

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)

Wei Yuan, George D Glekas, George M Allen, Hanna E Walukiewicz, Christopher V Rao, George W Ordal
The importance of the interaction of CheD with CheC and the chemoreceptors compared to its enzymatic activity during chemotaxis in Bacillus subtilis.
PLoS One: 2012, 7(12);e50689
[PubMed:23226535] [WorldCat.org] [DOI] (I p)

George D Glekas, Matthew J Plutz, Hanna E Walukiewicz, George M Allen, Christopher V Rao, George W Ordal
Elucidation of the multiple roles of CheD in Bacillus subtilis chemotaxis.
Mol Microbiol: 2012, 86(3);743-56
[PubMed:22931217] [WorldCat.org] [DOI] (I p)

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)

Kang Wu, Hanna E Walukiewicz, George D Glekas, George W Ordal, Christopher V Rao
Attractant binding induces distinct structural changes to the polar and lateral signaling clusters in Bacillus subtilis chemotaxis.
J Biol Chem: 2011, 286(4);2587-95
[PubMed:21098025] [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)

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)

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)

Michael A Zimmer, Hendrik Szurmant, Michael M Saulmon, Marissa A Collins, Jason S Bant, George W Ordal
The role of heterologous receptors in McpB-mediated signalling in Bacillus subtilis chemotaxis.
Mol Microbiol: 2002, 45(2);555-68
[PubMed:12123464] [WorldCat.org] [DOI] (P p)

Liam F Garrity, George W Ordal
Activation of the CheA kinase by asparagine in Bacillus subtilis chemotaxis.
Microbiology (Reading): 1997, 143(Pt 9);2945-2951
[PubMed:12094812] [WorldCat.org] [DOI] (P p)

J R Kirby, C J Kristich, M M Saulmon, M A Zimmer, L F Garrity, I B Zhulin, G W Ordal
CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis in Bacillus subtilis.
Mol Microbiol: 2001, 42(3);573-85
[PubMed:11722727] [WorldCat.org] [DOI] (P p)

E Karatan, M M Saulmon, M W Bunn, G W Ordal
Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis.
J Biol Chem: 2001, 276(47);43618-26
[PubMed:11553614] [WorldCat.org] [DOI] (P p)

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)

L F Garrity, S L Schiel, R Merrill, J Reizer, M H Saier, G W Ordal
Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC.
J Bacteriol: 1998, 180(17);4475-80
[PubMed:9721285] [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)

M M Rosario, G W Ordal
CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins.
Mol Microbiol: 1996, 21(3);511-8
[PubMed:8866475] [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 K Fuhrer, G W Ordal
Bacillus subtilis CheN, a homolog of CheA, the central regulator of chemotaxis in Escherichia coli.
J Bacteriol: 1991, 173(23);7443-8
[PubMed:1938941] [WorldCat.org] [DOI] (P p)

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