McpA

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  • 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
Interactions involving this protein in SubtInteract: McpA
MW, pI 72 kDa, 4.988
Gene length, protein length 1983 bp, 661 aa
Immediate neighbours tlpB, tlpA
Sequences Protein DNA Advanced_DNA
Genetic context
McpA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
McpA 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: BSU31240

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): McpB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • deamination of Gln-586, Gln-593, and Gln-594 (by CheD) PubMed
  • 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, 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:

Labs working on this gene/protein

Your additional remarks

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)