CheW

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  • Description: modulation of CheA activity in response to attractants, scaffold protein: facilitates coupling between CheA and receptors

Gene name cheW
Synonyms
Essential no
Product CheA modulator
Function control of CheA activity
Gene expression levels in SubtiExpress: cheW
MW, pI 17 kDa, 4.422
Gene length, protein length 468 bp, 156 aa
Immediate neighbours cheA, cheC
Sequences Protein DNA DNA_with_flanks
Genetic context
CheW context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CheW expression.png















Categories containing this gene/protein

motility and chemotaxis

This gene is a member of the following regulons

CodY regulon, DegU regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16440

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): CheV (N-terminal domain)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • cytoplasm (according to Swiss-Prot)
    • predominantly present at the cell poles PubMed

Database entries

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

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • in minimal medium, CheW is present with 2,100 +/- 430 molecules per cell PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 840 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1423 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1996 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1296 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 699 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)

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)

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)

Michael W Bunn, George W Ordal
Receptor conformational changes enhance methylesterase activity during chemotaxis by Bacillus subtilis.
Mol Microbiol: 2004, 51(3);721-8
[PubMed:14731274] [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)

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, K L Fredrick, G W Ordal, J D Helmann
Chemotaxis in Bacillus subtilis requires either of two functionally redundant CheW homologs.
J Bacteriol: 1994, 176(9);2736-9
[PubMed:8169224] [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 W Hanlon, P B Carpenter, G W Ordal
Influence of attractants and repellents on methyl group turnover on methyl-accepting chemotaxis proteins of Bacillus subtilis and role of CheW.
J Bacteriol: 1992, 174(13);4218-22
[PubMed:1624415] [WorldCat.org] [DOI] (P p)

D W Hanlon, L M Márquez-Magaña, P B Carpenter, M J Chamberlin, G W Ordal
Sequence and characterization of Bacillus subtilis CheW.
J Biol Chem: 1992, 267(17);12055-60
[PubMed:1601874] [WorldCat.org] (P p)

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