CheV

• Description: modulation of CheA activity in response to attractants
  
  

Gene name	cheV
Synonyms
Essential	no
Product	CheA modulator
Function	control of CheA activity
Gene expression levels in SubtiExpress: cheV
Interactions involving this protein in SubtInteract: CheV
MW, pI	34 kDa, 4.617
Gene length, protein length	909 bp, 303 aa
Immediate neighbours	ykzT, ykyB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription factors and their control, phosphoproteins, motility and chemotaxis

This gene is a member of the following regulons

SigD regulon

The gene

Basic information

• Locus tag: BSU14010

Phenotypes of a mutant

• cheV cheW double mutants exhibit complete loss of chemotaxis PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): CheW (N-terminal domain of CheV)

Extended information on the protein

• Kinetic information:

• Domains: N-terminal CheW-like domain, C-terminal two-component receiver domain PubMed

• Modification: the C-terminal two-component receiver domain is phosphorylated on a Asp residue by CheA PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • CheA-CheY PubMed

• Localization:
  • forms lateral clusters (phosphorylated form), but in the presence of high asparagine concentration (non-phosphorylated form) there is a reversible re-localization to the poles of the cell PubMed

Database entries

• Structure:

• UniProt: P37599

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: cheV PubMed

• Expression browser: cheV PubMed

• Sigma factor: SigD PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • in minimal medium, CheV is present with 7,500 +/- 2,000 molecules per cell PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)

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)

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)

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)

K L Fredrick, J D Helmann
Dual chemotaxis signaling pathways in Bacillus subtilis: a sigma D-dependent gene encodes a novel protein with both CheW and CheY homologous domains.
J Bacteriol: 1994, 176(9);2727-35
[PubMed:8169223] [WorldCat.org] [DOI] (P p)