FapR

• 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

Categories containing this gene/protein

biosynthesis of lipids, transcription factors and their control

This gene is a member of the following regulons

ComA regulon, FapR regulon

The gene

Basic information

• Locus tag: BSU15880

Database entries

• BsubCyc: BSU15880

• 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 and malonyl-ACP act as the molecular inducer of the FapR regulon PubMed

• Interactions:
  • malonyl-ACP-FapR PubMed

• Localization:

Database entries

• BsubCyc: BSU15880

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

• UniProt: O34835

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: fapR-plsX-fabD-fabG-acpA PubMed

• Expression browser: fapR PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed in the absence of malonyl-CoA or malonyl-ACP (FapR) PubMed
  • expressed at high cell density (ComA) PubMed

• Regulatory mechanism:
  • ComA: transcription activation (ComA) PubMed
  • FapR: transcription repression PubMed

• 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:

References

Other original publications

Additional publications: PubMed

Mariano A Martinez, María-Eugenia Zaballa, Francis Schaeffer, Marco Bellinzoni, Daniela Albanesi, Gustavo E Schujman, Alejandro J Vila, Pedro M Alzari, Diego de Mendoza
A novel role of malonyl-ACP in lipid homeostasis.
Biochemistry: 2010, 49(14);3161-7
[PubMed:20201588] [WorldCat.org] [DOI] (I p)

Mariano A Martinez, Diego de Mendoza, Gustavo E Schujman
Transcriptional and functional characterization of the gene encoding acyl carrier protein in Bacillus subtilis.
Microbiology (Reading): 2010, 156(Pt 2);484-495
[PubMed:19850612] [WorldCat.org] [DOI] (I p)

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)

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)

Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051] [WorldCat.org] [DOI] (P p)