Difference between revisions of "FabD"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[plsX]]'', ''[[fabG]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[plsX]]'', ''[[fabG]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15900 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15900 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15900 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15900 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15900 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15900 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:fabD_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:fabD_context.gif]]

Revision as of 10:12, 14 May 2013

  • 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
Gene expression levels in SubtiExpress: fabD
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
Sequences Protein DNA DNA_with_flanks
Genetic context
FabD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FabD expression.png




























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

Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903] [WorldCat.org] [DOI] (P p)

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)