Difference between revisions of "CheV"

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(Biological materials)
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* '''Mutant:'''
 
* '''Mutant:'''
** DS70 (mls in NCIB3610) {{PubMed|12864845}}
+
** DS70 (''cheV''::''mls'' in NCIB3610) {{PubMed|12864845}}
** TB183 ''amyE''::Phy-''sfgfp'' (mls in NCIB3610 with constitutive expressed ''sfgfp'') {{PubMed|26122431}}
+
** TB183 ''amyE''::Phy-''sfgfp'' (''cheV''::''mls'' in NCIB3610 with constitutive expressed ''sfgfp'') {{PubMed|26122431}}
** TB199 ''amyE''::Phy-''mKATE2'' (mls in NCIB3610 with constitutive expressed ''mKATE2'') {{PubMed|26122431}}
+
** TB199 ''amyE''::Phy-''mKATE2'' (''cheV''::''mls'' in NCIB3610 with constitutive expressed ''mKATE2'') {{PubMed|26122431}}
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 07:18, 3 July 2015

  • 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, kre
Sequences Protein DNA DNA_with_flanks
Genetic context
CheV context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CheV expression.png















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
  • not essential for pellicle biofilm formation, but mutant is outcompeted by the wild-type strain when competed during pellicle formation PubMed

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:
  • 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:
  • 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:
  • 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
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1117 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1764 PubMed

Biological materials

  • Mutant:
    • DS70 (cheV::mls in NCIB3610) PubMed
    • TB183 amyE::Phy-sfgfp (cheV::mls in NCIB3610 with constitutive expressed sfgfp) PubMed
    • TB199 amyE::Phy-mKATE2 (cheV::mls in NCIB3610 with constitutive expressed mKATE2) PubMed
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Christopher V Rao, George D Glekas, George W Ordal
The three adaptation systems of Bacillus subtilis chemotaxis.
Trends Microbiol.: 2008, 16(10);480-7
[PubMed:18774298] [WorldCat.org] [DOI] (P p)

Original publications

Theresa Hölscher, Benjamin Bartels, Yu-Cheng Lin, Ramses Gallegos-Monterrosa, Alexa Price-Whelan, Roberto Kolter, Lars E P Dietrich, Ákos T Kovács
Motility, Chemotaxis and Aerotaxis Contribute to Competitiveness during Bacterial Pellicle Biofilm Development.
J. Mol. Biol.: 2015, 427(23);3695-3708
[PubMed:26122431] [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)

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)

Daniel B Kearns, Richard Losick
Swarming motility in undomesticated Bacillus subtilis.
Mol. Microbiol.: 2003, 49(3);581-90
[PubMed:12864845] [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)