FapR

From SubtiWiki
Revision as of 06:26, 3 July 2009 by Jstuelk (talk | contribs) (The protein)
Jump to: navigation, search
  • 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
YlpC context.gif
This image was kindly provided by SubtiList



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, acts as the molecular inducer of the FapR regulon
  • Interactions:
  • Localization:

Database entries

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

Additional information

Expression and regulation

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

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)