FapR

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  • 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
YlpC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FapR expression.png

Contents















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 FapR regulon

The gene

Basic information

  • Locus tag: BSU15880

Phenotypes of a mutant

Database entries

  • 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

  • Structure: 2F3X (complex with effector), 2F41
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

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

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] (P p)

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, Engl.): 2010, 156(Pt 2);484-95
[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;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)

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