McpC

• Description: membrane-bound chemotaxis receptor, 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
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 This image was kindly provided by SubtiList

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • cell membrane PubMed

Database entries

• Structure:

• UniProt: P54576

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: mcpC PubMed

• Expression browser: mcpC PubMed

• Sigma factor: SigD PubMed

• 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:

References

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)

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)