Difference between revisions of "ComFA"
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** [[ComGA]]-[[ComFA]] {{PubMed|17630974}} | ** [[ComGA]]-[[ComFA]] {{PubMed|17630974}} | ||
** [[ComEC]]-[[ComFA]] {{PubMed|17630974}} | ** [[ComEC]]-[[ComFA]] {{PubMed|17630974}} | ||
− | ** [[ | + | ** [[CoiA]]-[[ComFA]] {{PubMed|17630974}} |
** [[SsbB]]-[[ComFA]] {{PubMed|17630974}} | ** [[SsbB]]-[[ComFA]] {{PubMed|17630974}} | ||
** [[DprA]]-[[ComFA]] {{PubMed|17630974}} | ** [[DprA]]-[[ComFA]] {{PubMed|17630974}} |
Revision as of 16:12, 8 April 2011
- Description: late competence protein required for DNA binding and uptake
Gene name | comFA |
Synonyms | |
Essential | no |
Product | ATP-binding protein |
Function | genetic competence |
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
MW, pI | 52 kDa, 9.824 |
Gene length, protein length | 1389 bp, 463 aa |
Immediate neighbours | comFB, yviA |
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, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35470
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: helicase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P39145
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Original publications
Additional publications: PubMed
Miriam Kaufenstein, Martin van der Laan, Peter L Graumann
The three-layered DNA uptake machinery at the cell pole in competent Bacillus subtilis cells is a stable complex.
J Bacteriol: 2011, 193(7);1633-42
[PubMed:21278288]
[WorldCat.org]
[DOI]
(I p)
Naomi Kramer, Jeanette Hahn, David Dubnau
Multiple interactions among the competence proteins of Bacillus subtilis.
Mol Microbiol: 2007, 65(2);454-64
[PubMed:17630974]
[WorldCat.org]
[DOI]
(P p)
Jeanette Hahn, Berenike Maier, Bert Jan Haijema, Michael Sheetz, David Dubnau
Transformation proteins and DNA uptake localize to the cell poles in Bacillus subtilis.
Cell: 2005, 122(1);59-71
[PubMed:16009133]
[WorldCat.org]
[DOI]
(P p)
Hanne Jarmer, Randy Berka, Steen Knudsen, Hans H Saxild
Transcriptome analysis documents induced competence of Bacillus subtilis during nitrogen limiting conditions.
FEMS Microbiol Lett: 2002, 206(2);197-200
[PubMed:11814663]
[WorldCat.org]
[DOI]
(P p)
J A Londoño-Vallejo, D Dubnau
Mutation of the putative nucleotide binding site of the Bacillus subtilis membrane protein ComFA abolishes the uptake of DNA during transformation.
J Bacteriol: 1994, 176(15);4642-5
[PubMed:8045895]
[WorldCat.org]
[DOI]
(P p)
J A Londoño-Vallejo, D Dubnau
Membrane association and role in DNA uptake of the Bacillus subtilis PriA analogue ComF1.
Mol Microbiol: 1994, 13(2);197-205
[PubMed:7984101]
[WorldCat.org]
[DOI]
(P p)
J A Londoño-Vallejo, D Dubnau
comF, a Bacillus subtilis late competence locus, encodes a protein similar to ATP-dependent RNA/DNA helicases.
Mol Microbiol: 1993, 9(1);119-31
[PubMed:8412657]
[WorldCat.org]
[DOI]
(P p)