Difference between revisions of "FabD"

From SubtiWiki
Jump to: navigation, search
m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
Line 104: Line 104:
 
* '''Operon:''' ''[[fapR]]-[[plsX]]-[[fabD]]-[[fabG]]-[[acpA]]'' {{PubMed|12737802,19850612}}
 
* '''Operon:''' ''[[fapR]]-[[plsX]]-[[fabD]]-[[fabG]]-[[acpA]]'' {{PubMed|12737802,19850612}}
  
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|16932747}}
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fabD_1663567_1664520_1 fabD] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:''' [[SigA]] {{PubMed|16932747}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 114: Line 116:
 
** [[FapR]]: transcription repression {{PubMed|12737802}}
 
** [[FapR]]: transcription repression {{PubMed|12737802}}
  
* '''Additional information:'''  
+
* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =

Revision as of 08:50, 13 April 2012

  • Description: malonyl CoA-acyl carrier protein transacylase

Gene name fabD
Synonyms ylpE
Essential yes PubMed
Product malonyl CoA-acyl carrier protein transacylase
Function fatty acid biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis
MW, pI 33 kDa, 4.515
Gene length, protein length 951 bp, 317 aa
Immediate neighbours plsX, fabG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FabD context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

ComA regulon, FapR regulon

The gene

Basic information

  • Locus tag: BSU15900

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein] (according to Swiss-Prot)
  • Protein family: fabD family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced if the cells experience an accumulation of malonyl-CoA (FapR) PubMed
    • expressed at high cell density (ComA) PubMed
  • 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

Original Publications

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)

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)

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)

L Serre, E C Verbree, Z Dauter, A R Stuitje, Z S Derewenda
The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
J Biol Chem: 1995, 270(22);12961-4
[PubMed:7768883] [WorldCat.org] [DOI] (P p)