Difference between revisions of "ComC"
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− | * '''Description:''' late competence gene required for processing and translocation of [[ComGC]], [[ComGD]], [[ComGE]] and [[ComGG]] | + | * '''Description:''' late competence gene required for processing and translocation of [[ComGC]], [[ComGD]], [[ComGE]] and [[ComGG]] {{PubMed|9723928}} <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Product''' || processing protease | |style="background:#ABCDEF;" align="center"| '''Product''' || processing protease | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || genetic | + | |style="background:#ABCDEF;" align="center"|'''Function''' || [[genetic competence]] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | ||
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine (according to Swiss-Prot) | + | * '''Catalyzed reaction/ biological activity:''' |
+ | ** processing and translocation of [[ComGC]], [[ComGD]], [[ComGE]] and [[ComGG]] {{PubMed|9723928}} | ||
+ | ** Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine (according to Swiss-Prot) | ||
* '''Protein family:''' peptidase A24 family (according to Swiss-Prot) | * '''Protein family:''' peptidase A24 family (according to Swiss-Prot) | ||
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* '''Interactions:''' | * '''Interactions:''' | ||
− | ** [[ComC]]-[[ComGC]] {{PubMed| | + | ** [[ComC]]-[[ComGC]] {{PubMed|9723928}} |
− | ** [[ComC]]-[[ComGD]] {{PubMed| | + | ** [[ComC]]-[[ComGD]] {{PubMed|9723928}} |
− | ** [[ComC]]-[[ComGE]] {{PubMed| | + | ** [[ComC]]-[[ComGE]] {{PubMed|9723928}} |
− | ** [[ComC]]-[[ComGG]] {{PubMed| | + | ** [[ComC]]-[[ComGG]] {{PubMed|9723928}} |
* '''Localization:''' cell membrane (according to Swiss-Prot) | * '''Localization:''' cell membrane (according to Swiss-Prot) |
Revision as of 15:13, 8 April 2011
- Description: late competence gene required for processing and translocation of ComGC, ComGD, ComGE and ComGG PubMed
Gene name | comC |
Synonyms | |
Essential | no |
Product | processing protease |
Function | genetic competence |
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
MW, pI | 26 kDa, 9.843 |
Gene length, protein length | 744 bp, 248 aa |
Immediate neighbours | spoIIB, folC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
genetic competence, protein secretion, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28070
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- processing and translocation of ComGC, ComGD, ComGE and ComGG PubMed
- Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine (according to Swiss-Prot)
- Protein family: peptidase A24 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P15378
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: comC PubMed
- Regulation:
- 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
Inês Chen, David Dubnau
DNA uptake during bacterial transformation.
Nat Rev Microbiol: 2004, 2(3);241-9
[PubMed:15083159]
[WorldCat.org]
[DOI]
(P p)
Original publications
Inês Chen, Roberta Provvedi, David Dubnau
A macromolecular complex formed by a pilin-like protein in competent Bacillus subtilis.
J Biol Chem: 2006, 281(31);21720-21727
[PubMed:16751195]
[WorldCat.org]
[DOI]
(P p)
Y S Chung, F Breidt, D Dubnau
Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis.
Mol Microbiol: 1998, 29(3);905-13
[PubMed:9723928]
[WorldCat.org]
[DOI]
(P p)
Y S Chung, D Dubnau
ComC is required for the processing and translocation of comGC, a pilin-like competence protein of Bacillus subtilis.
Mol Microbiol: 1995, 15(3);543-51
[PubMed:7783624]
[WorldCat.org]
[DOI]
(P p)
D van Sinderen, A ten Berge, B J Hayema, L Hamoen, G Venema
Molecular cloning and sequence of comK, a gene required for genetic competence in Bacillus subtilis.
Mol Microbiol: 1994, 11(4);695-703
[PubMed:8196543]
[WorldCat.org]
[DOI]
(P p)
S Mohan, D Dubnau
Transcriptional regulation of comC: evidence for a competence-specific transcription factor in Bacillus subtilis.
J Bacteriol: 1990, 172(7);4064-71
[PubMed:1694528]
[WorldCat.org]
[DOI]
(P p)
S Mohan, J Aghion, N Guillen, D Dubnau
Molecular cloning and characterization of comC, a late competence gene of Bacillus subtilis.
J Bacteriol: 1989, 171(11);6043-51
[PubMed:2553669]
[WorldCat.org]
[DOI]
(P p)