McpC

• 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
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

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:
  • deaminated McpC stimulates phosphorylation of CheA PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • deamination of Gln-609 (by CheD) PubMed, deaminated McpC stimulates phosphorylation of CheA PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • CheD-McpC, deamination of Gln-609 in McpC PubMed
  • McpC-ArtP, for chemotaxis to lysine and arginine PubMed
  • McpC-MetQ, for chemotaxis to methionine PubMed
  • McpC-YckB, for chemotaxis to tryptophan PubMed

• 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

Additional publications: PubMed

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)

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)