Difference between revisions of "FapR"

From SubtiWiki
Jump to: navigation, search
Line 39: Line 39:
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
<br/><br/><br/><br/>
+
<br/><br/>
<br/><br/><br/><br/>
 
 
 
 
 
<br/><br/><br/><br/><br/><br/>
 
  
 
= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
Line 150: Line 146:
 
<pubmed>12737802, </pubmed>
 
<pubmed>12737802, </pubmed>
 
==Other original publications==
 
==Other original publications==
<pubmed>18941141, 18820022, 18384517, 16932747,19850612 16091051 20201588</pubmed>
+
<pubmed>18941141, 18820022, 18384517, 16932747,19850612 16091051 20201588 23102226 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:28, 31 October 2012

  • 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:
Lipid synthesis
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
Expression at a glance   PubMed
FapR expression.png















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:
  • 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

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

Jessica M Ellis, Michael J Wolfgang
A genetically encoded metabolite sensor for malonyl-CoA.
Chem Biol: 2012, 19(10);1333-9
[PubMed:23102226] [WorldCat.org] [DOI] (I p)

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)