Difference between revisions of "AcpA"

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* '''Regulation:'''  
 
* '''Regulation:'''  
 
** ''[[fapR]]'': repressed in the absence of malonyl-CoA or malonyl-[[AcpA|ACP]] ([[FapR]]) {{PubMed|12737802}}
 
** ''[[fapR]]'': repressed in the absence of malonyl-CoA or malonyl-[[AcpA|ACP]] ([[FapR]]) {{PubMed|12737802}}
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** strongly repressed in response to glucose starvation in M9 medium {{PubMed|23033921}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
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==Original Publications==
 
==Original Publications==
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'''Additional publications:''' {{PubMed|23033921}}
 
<pubmed>10997907,19850612, 12737802 18838690 20201588 </pubmed>
 
<pubmed>10997907,19850612, 12737802 18838690 20201588 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:35, 8 October 2012

  • Description: acyl carrier protein

Gene name acpA
Synonyms acpP
Essential yes PubMed
Product acyl carrier protein
Function fatty acid biosynthesis
Gene expression levels in SubtiExpress: acpA
Interactions involving this protein in SubtInteract: AcpA
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis
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
Expression at a glance   PubMed
AcpA expression.png



















Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

FapR regulon

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

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • fapR: repressed in the absence of malonyl-CoA or malonyl-ACP (FapR) PubMed
    • strongly repressed in response to glucose starvation in M9 medium 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

Additional publications: PubMed

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)

Max J Cryle, Ilme Schlichting
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
Proc Natl Acad Sci U S A: 2008, 105(41);15696-701
[PubMed:18838690] [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)