Difference between revisions of "McpC"

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=References=
 
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'''Additional publications:''' {{PubMed|23038252}}
 
'''Additional publications:''' {{PubMed|23038252}}
<pubmed>21515776 22931217 </pubmed>
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<pubmed>22931217</pubmed>
 
<pubmed>15317802,8251536,9353924,15544802,6137212,9721285,2505839,2105313,12603740,23038252,18763711 9721285, </pubmed>
 
<pubmed>15317802,8251536,9353924,15544802,6137212,9721285,2505839,2105313,12603740,23038252,18763711 9721285, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:23, 8 October 2012

  • Description: membrane-bound chemotaxis receptor for proline, methyl-accepting chemotaxis protein

Gene name mcpC
Synonyms prg71
Essential no
Product methyl-accepting chemotaxis protein
Function control of chemotaxis
threonine, glycine, serine, lysine, valine and arginine
Gene expression levels in SubtiExpress: mcpC
Interactions involving this protein in SubtInteract: McpC
MW, pI 71 kDa, 5.174
Gene length, protein length 1962 bp, 654 aa
Immediate neighbours ykwB, ykwC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
McpC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
McpC expression.png

















Categories containing this gene/protein

motility and chemotaxis, membrane proteins

This gene is a member of the following regulons

SigD regulon

The gene

Basic information

  • Locus tag: BSU13950

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):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • in minimal medium, McpC is present with 2,800 +/- 640 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

Additional publications: PubMed

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)

George D Glekas, Matthew J Plutz, Hanna E Walukiewicz, George M Allen, Christopher V Rao, George W Ordal
Elucidation of the multiple roles of CheD in Bacillus subtilis chemotaxis.
Mol Microbiol: 2012, 86(3);743-56
[PubMed:22931217] [WorldCat.org] [DOI] (I p)

George D Glekas, Brendan J Mulhern, Abigail Kroc, Keegan A Duelfer, Victor Lei, Christopher V Rao, George W Ordal
The Bacillus subtilis chemoreceptor McpC senses multiple ligands using two discrete mechanisms.
J Biol Chem: 2012, 287(47);39412-8
[PubMed:23038252] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Hendrik Szurmant, Michael W Bunn, Stephen H Cho, George W Ordal
Ligand-induced conformational changes in the Bacillus subtilis chemoreceptor McpB determined by disulfide crosslinking in vivo.
J Mol Biol: 2004, 344(4);919-28
[PubMed:15544802] [WorldCat.org] [DOI] (P p)

Christopher J Kristich, George W Ordal
Analysis of chimeric chemoreceptors in Bacillus subtilis reveals a role for CheD in the function of the McpC HAMP domain.
J Bacteriol: 2004, 186(17);5950-5
[PubMed:15317802] [WorldCat.org] [DOI] (P p)

Christopher J Kristich, George D Glekas, George W Ordal
The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis.
Mol Microbiol: 2003, 47(5);1353-66
[PubMed:12603740] [WorldCat.org] [DOI] (P p)

L F Garrity, S L Schiel, R Merrill, J Reizer, M H Saier, G W Ordal
Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC.
J Bacteriol: 1998, 180(17);4475-80
[PubMed:9721285] [WorldCat.org] [DOI] (P p)

Jakob Müller, Stacey Schiel, George W Ordal, Hans H Saxild
Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis.
Microbiology (Reading): 1997, 143 ( Pt 10);3231-3240
[PubMed:9353924] [WorldCat.org] [DOI] (P p)

D W Hanlon, C Ying, G W Ordal
Purification and reconstitution of the methyl-accepting chemotaxis proteins from Bacillus subtilis.
Biochim Biophys Acta: 1993, 1158(3);345-51
[PubMed:8251536] [WorldCat.org] [DOI] (P p)

M S Thoelke, J M Casper, G W Ordal
Methyl group turnover on methyl-accepting chemotaxis proteins during chemotaxis by Bacillus subtilis.
J Biol Chem: 1990, 265(4);1928-32
[PubMed:2105313] [WorldCat.org] (P p)

M S Thoelke, J R Kirby, G W Ordal
Novel methyl transfer during chemotaxis in Bacillus subtilis.
Biochemistry: 1989, 28(13);5585-9
[PubMed:2505839] [WorldCat.org] [DOI] (P p)

J A Ahlgren, G W Ordal
Methyl esterification of glutamic acid residues of methyl-accepting chemotaxis proteins in Bacillus subtilis.
Biochem J: 1983, 213(3);759-63
[PubMed:6137212] [WorldCat.org] [DOI] (P p)