ComP
- Description: two-component sensor kinase, detects extracellular ComX
Gene name | comP |
Synonyms | |
Essential | no |
Product | two-component sensor kinase |
Function | regulation of genetic competence and quorum sensing |
Interactions involving this protein in SubtInteract: ComP | |
MW, pI | 89 kDa, 7.997 |
Gene length, protein length | 2307 bp, 769 aa |
Immediate neighbours | comA, comX |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
genetic competence, protein modification, transcription factors and their control, quorum sensing, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31690
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of ComA
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains: eight transmembrane segments
- Modification: autophosphorylation on a His residue
- Cofactor(s):
- Effectors of protein activity: ComX (extracellular)
- Localization: cell membrane PubMed
Database entries
- Structure:
- UniProt: Q99027
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: comP PubMed
- 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
Reviews
Leendert W Hamoen, Gerard Venema, Oscar P Kuipers
Controlling competence in Bacillus subtilis: shared use of regulators.
Microbiology (Reading): 2003, 149(Pt 1);9-17
[PubMed:12576575]
[WorldCat.org]
[DOI]
(P p)
Original Publications
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)
Mireille Ansaldi, Darja Marolt, Tina Stebe, Ines Mandic-Mulec, David Dubnau
Specific activation of the Bacillus quorum-sensing systems by isoprenylated pheromone variants.
Mol Microbiol: 2002, 44(6);1561-73
[PubMed:12067344]
[WorldCat.org]
[DOI]
(P p)
P Tortosa, L Logsdon, B Kraigher, Y Itoh, I Mandic-Mulec, D Dubnau
Specificity and genetic polymorphism of the Bacillus competence quorum-sensing system.
J Bacteriol: 2001, 183(2);451-60
[PubMed:11133937]
[WorldCat.org]
[DOI]
(P p)
F Piazza, P Tortosa, D Dubnau
Mutational analysis and membrane topology of ComP, a quorum-sensing histidine kinase of Bacillus subtilis controlling competence development.
J Bacteriol: 1999, 181(15);4540-8
[PubMed:10419951]
[WorldCat.org]
[DOI]
(P p)
C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672]
[WorldCat.org]
[DOI]
(P p)
Bauke Oudega, Gregory Koningstein, Luísa Rodrigues, Maria de Sales Ramon, Helmut Hilbert, Andreas Düsterhöft, Thomas M Pohl, Thomas Weitzenegger
Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).
Microbiology (Reading): 1997, 143 ( Pt 8);2769-2774
[PubMed:9274030]
[WorldCat.org]
[DOI]
(P p)
M Perego, J A Hoch
Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(4);1549-53
[PubMed:8643670]
[WorldCat.org]
[DOI]
(P p)
Y Weinrauch, R Penchev, E Dubnau, I Smith, D Dubnau
A Bacillus subtilis regulatory gene product for genetic competence and sporulation resembles sensor protein members of the bacterial two-component signal-transduction systems.
Genes Dev: 1990, 4(5);860-72
[PubMed:2116363]
[WorldCat.org]
[DOI]
(P p)