FapR
Revision as of 14:19, 17 April 2014 by 134.76.70.252 (talk)
- Description: repressor of fatty acid synthetic genes
Gene name | fapR |
Synonyms | ylpC |
Essential | no |
Product | transcriptional repressor |
Function | regulation of fatty acid biosynthesis |
Gene expression levels in SubtiExpress: fapR | |
Interactions involving this protein in SubtInteract: FapR | |
Metabolic function and regulation of this protein in SubtiPathways: fapR | |
MW, pI | 21 kDa, 5.393 |
Gene length, protein length | 564 bp, 188 aa |
Immediate neighbours | recG, plsX |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis of lipids, transcription factors and their control
This gene is a member of the following regulons
The FapR regulon
The gene
Basic information
- Locus tag: BSU15880
Phenotypes of a mutant
Database entries
- BsubCyc: BSU15880
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: FapR regulates the expression of at least 10 genes (the fap regulon). It autoregulates its own expression. Malonyl-CoA, a precursor of fatty acid biosynthesis, binds to FapR changing its conformation to a non-DNA binding state. Hence, conditions that cause malonyl-CoA accumulation, like fatty acid biosynthesis inhibition, derepress the fap regulon.
- Protein family: fapR family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: malonyl-CoA and malonyl-ACP act as the molecular inducer of the FapR regulon PubMed
Database entries
- BsubCyc: BSU15880
- UniProt: O34835
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 85 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 490 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 412 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 729 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287]
[WorldCat.org]
[DOI]
(P p)
The FapR regulon
Other original publications
Additional publications: PubMed