Difference between revisions of "McpB"
(→Extended information on the protein) |
|||
| Line 66: | Line 66: | ||
* '''Domains:''' | * '''Domains:''' | ||
| − | * '''Modification:''' | + | * '''Modification:''' methylated at residues Gln371, Glu630, and Glu637 {{PubMed|20864474}} |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
| Line 119: | Line 119: | ||
=References= | =References= | ||
| − | <pubmed>11722727,10825179,8251536,12909020,10196193,15544802,6137212,9194713,2505839,8188684,2105313,12123464,14731274,,18763711, 19864420 </pubmed> | + | <pubmed>11722727,10825179,8251536,12909020,10196193,15544802,6137212,9194713,2505839,8188684,2105313,12123464,14731274,20864474 ,18763711, 19864420 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 17:22, 25 September 2010
- Description: methyl-accepting chemotaxis protein
| Gene name | mcpB |
| Synonyms | |
| Essential | no |
| Product | methyl-accepting chemotaxis protein |
| Function | control of chemotaxis |
| MW, pI | 71 kDa, 5.13 |
| Gene length, protein length | 1986 bp, 662 aa |
| Immediate neighbours | tlpA, tgl |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU31260
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: K(D) for asparagine: 14 myM PubMed
- Domains:
- Modification: methylated at residues Gln371, Glu630, and Glu637 PubMed
- Cofactor(s):
- Effectors of protein activity: asparagine (binds to the part of McpB that is exposed to the exterior) PubMed
- Localization: cell membrane PubMed
Database entries
- Structure:
- UniProt: P39215
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
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, Joseph R Cates, Theodore M Cohen, Christopher V Rao, George W Ordal
Site-specific methylation in Bacillus subtilis chemotaxis: effect of covalent modifications to the chemotaxis receptor McpB.
Microbiology (Reading): 2011, 157(Pt 1);56-65
[PubMed:20864474]
[WorldCat.org]
[DOI]
(I p)
George D Glekas, Richard M Foster, Joseph R Cates, Jeffrey A Estrella, Michael J Wawrzyniak, Christopher V Rao, George W Ordal
A PAS domain binds asparagine in the chemotaxis receptor McpB in Bacillus subtilis.
J Biol Chem: 2010, 285(3);1870-8
[PubMed:19864420]
[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)
Michael W Bunn, George W Ordal
Receptor conformational changes enhance methylesterase activity during chemotaxis by Bacillus subtilis.
Mol Microbiol: 2004, 51(3);721-8
[PubMed:14731274]
[WorldCat.org]
[DOI]
(P p)
Michael W Bunn, George W Ordal
Transmembrane organization of the Bacillus subtilis chemoreceptor McpB deduced by cysteine disulfide crosslinking.
J Mol Biol: 2003, 331(4);941-9
[PubMed:12909020]
[WorldCat.org]
[DOI]
(P p)
Michael A Zimmer, Hendrik Szurmant, Michael M Saulmon, Marissa A Collins, Jason S Bant, George W Ordal
The role of heterologous receptors in McpB-mediated signalling in Bacillus subtilis chemotaxis.
Mol Microbiol: 2002, 45(2);555-68
[PubMed:12123464]
[WorldCat.org]
[DOI]
(P p)
J R Kirby, C J Kristich, M M Saulmon, M A Zimmer, L F Garrity, I B Zhulin, G W Ordal
CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis in Bacillus subtilis.
Mol Microbiol: 2001, 42(3);573-85
[PubMed:11722727]
[WorldCat.org]
[DOI]
(P p)
M A Zimmer, J Tiu, M A Collins, G W Ordal
Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation.
J Biol Chem: 2000, 275(32);24264-72
[PubMed:10825179]
[WorldCat.org]
[DOI]
(P p)
J R Kirby, M M Saulmon, C J Kristich, G W Ordal
CheY-dependent methylation of the asparagine receptor, McpB, during chemotaxis in Bacillus subtilis.
J Biol Chem: 1999, 274(16);11092-100
[PubMed:10196193]
[WorldCat.org]
[DOI]
(P p)
J R Kirby, C J Kristich, S L Feinberg, G W Ordal
Methanol production during chemotaxis to amino acids in Bacillus subtilis.
Mol Microbiol: 1997, 24(4);869-78
[PubMed:9194713]
[WorldCat.org]
[DOI]
(P 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)
