McpA

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

Gene name	mcpA
Synonyms
Essential	no
Product	methyl-accepting chemotaxis protein
Function	control of chemotaxis
Gene expression levels in SubtiExpress: mcpA
MW, pI	72 kDa, 4.988
Gene length, protein length	1983 bp, 661 aa
Immediate neighbours	tlpB, tlpA
Get the DNA and protein sequences (Barbe et al., 2009)
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: BSU31240

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): McpB

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • CheD-McpA, deamination of Gln-586, Gln-593 and Gln-594 in McpA PubMed

• Localization:
  • cell membrane PubMed

Database entries

• Structure:

• UniProt: P39214

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tlpA-mcpA PubMed

• Expression browser: mcpA PubMed

• Sigma factor: SigD PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • in minimal medium, McpA is present with 15,900 +/- 3,000 molecules per cell PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)

D W Hanlon, G W Ordal
Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis.
J Biol Chem: 1994, 269(19);14038-46
[PubMed:8188684] [WorldCat.org] (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)