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

  • 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

Hanna E Walukiewicz, Payman Tohidifar, George W Ordal, Christopher V Rao
Interactions among the three adaptation systems of Bacillus subtilis chemotaxis as revealed by an in vitro receptor-kinase assay.
Mol Microbiol: 2014, 93(6);1104-18
[PubMed:25039821] [WorldCat.org] [DOI] (I p)

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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