Difference between revisions of "McpC"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
* not essential for pellicle biofilm formation and mutant has similar fitness to the wild-type strain when competed during pellicle formation {{PubMed|26122431}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Mutant:'''
 
* '''Mutant:'''
 +
** DS180 (''mcpC''::''mls'' in NCIB3610) {{PubMed|12864845}}
 +
** TB184 ''amyE''::Phy-''sfgfp'' (''mcpC''::''mls'' in NCIB3610 with constitutive expressed ''sfgfp'') {{PubMed|26122431}}
 +
** TB200 ''amyE''::Phy-''mKATE2'' (''mcpC''::''mls'' in NCIB3610 with constitutive expressed ''mKATE2'') {{PubMed|26122431}}
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
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=References=
 
=References=
 
'''Additional publications:''' {{PubMed|22931217}}
 
'''Additional publications:''' {{PubMed|22931217}}
<pubmed>15317802,8251536,9353924,15544802,6137212,9721285,2505839,2105313,12603740,23038252,18763711 9721285, 21515776</pubmed>
+
<pubmed>12864845,26122431,15317802,8251536,9353924,15544802,6137212,9721285,2505839,2105313,12603740,23038252,18763711 9721285, 21515776</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:03, 2 July 2015

  • 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
McpC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
McpC 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: BSU13950

Phenotypes of a mutant

  • not essential for pellicle biofilm formation and mutant has similar fitness to the wild-type strain when competed during pellicle formation PubMed

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:
  • Domains:
  • 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, McpC is present with 2,800 +/- 640 molecules per cell PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 236 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 990 PubMed

Biological materials

  • Mutant:
    • DS180 (mcpC::mls in NCIB3610) PubMed
    • TB184 amyE::Phy-sfgfp (mcpC::mls in NCIB3610 with constitutive expressed sfgfp) PubMed
    • TB200 amyE::Phy-mKATE2 (mcpC::mls in NCIB3610 with constitutive expressed mKATE2) PubMed
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Theresa Hölscher, Benjamin Bartels, Yu-Cheng Lin, Ramses Gallegos-Monterrosa, Alexa Price-Whelan, Roberto Kolter, Lars E P Dietrich, Ákos T Kovács
Motility, Chemotaxis and Aerotaxis Contribute to Competitiveness during Bacterial Pellicle Biofilm Development.
J. Mol. Biol.: 2015, 427(23);3695-3708
[PubMed:26122431] [WorldCat.org] [DOI] (I p)

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)

Daniel B Kearns, Richard Losick
Swarming motility in undomesticated Bacillus subtilis.
Mol. Microbiol.: 2003, 49(3);581-90
[PubMed:12864845] [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)

J Müller, S Schiel, G W Ordal, H H Saxild
Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis.
Microbiology (Reading, Engl.): 1997, 143 ( Pt 10);3231-40
[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)