Difference between revisions of "AcpA"

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(Labs working on this gene/protein)
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=References=
 
=References=
 
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==Reviews==
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<pubmed> 15952903 </pubmed>
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==Original Publications==
 
<pubmed>10997907,19850612, 12737802</pubmed>
 
<pubmed>10997907,19850612, 12737802</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:13, 6 January 2010

  • Description: acyl carrier protein

Gene name acpA
Synonyms acpP
Essential yes PubMed
Product acyl carrier protein
Function fatty acid biosynthesis
MW, pI 8 kDa, 3.594
Gene length, protein length 231 bp, 77 aa
Immediate neighbours fabG, rnc
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AcpA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU15920

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot), during sporulation in the mother cell PubMed

Database entries

  • Structure: 1F80 (complex with AcpS), 3EJE (complex with BioI), 1HY8
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • fapR: induced if 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

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, 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)

K D Parris, L Lin, A Tam, R Mathew, J Hixon, M Stahl, C C Fritz, J Seehra, W S Somers
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Structure: 2000, 8(8);883-95
[PubMed:10997907] [WorldCat.org] [DOI] (P p)