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 |
Contents
Categories containing this gene/protein
transcription factors and their control, phosphoproteins, motility and chemotaxis
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14010
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): CheW (N-terminal domain of CheV)
Extended information on the protein
- Kinetic information:
- Modification: the C-terminal two-component receiver domain is phosphorylated on a Asp residue by CheA PubMed
- Cofactor(s):
- Effectors of protein activity:
- 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:
Additional information
Expression and regulation
- 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:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)