FapR

• Description: repressor of fatty acid synthetic genes
  
  

Gene name	fapR
Synonyms	ylpC
Essential	no
Product	transcriptional repressor
Function	regulation of fatty acid biosynthesis
MW, pI	21 kDa, 5.393
Gene length, protein length	564 bp, 188 aa
Immediate neighbours	recG, plsX
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU15880

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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, acts as the molecular inducer of the FapR regulon

• Interactions:

• Localization:

Database entries

• Structure: 2F3X (complex with effector), 2F41

• Swiss prot entry: O34835

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor: SigA

• Regulation:
  • repressed unless the cells experience an accumulation of malonyl-CoA (FapR) PubMed

• Regulatory mechanism:
  • FapR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Yong-Mei Zhang, Charles O Rock
Transcriptional regulation in bacterial membrane lipid synthesis.
J Lipid Res: 2009, 50 Suppl(Suppl);S115-9
[PubMed:18941141] [WorldCat.org] [DOI] (P p)

Letal I Salzberg, John D Helmann
Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition.
J Bacteriol: 2008, 190(23);7797-807
[PubMed:18820022] [WorldCat.org] [DOI] (I p)

Gustavo E Schujman, Silvia Altabe, Diego de Mendoza
A malonyl-CoA-dependent switch in the bacterial response to a dysfunction of lipid metabolism.
Mol Microbiol: 2008, 68(4);987-96
[PubMed:18384517] [WorldCat.org] [DOI] (I p)

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)

Gustavo E Schujman, Marcelo Guerin, Alejandro Buschiazzo, Francis Schaeffer, Leticia I Llarrull, Georgina Reh, Alejandro J Vila, Pedro M Alzari, Diego de Mendoza
Structural basis of lipid biosynthesis regulation in Gram-positive bacteria.
EMBO J: 2006, 25(17);4074-83
[PubMed:16932747] [WorldCat.org] [DOI] (P p)

Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802] [WorldCat.org] [DOI] (P p)