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
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, 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)