Difference between revisions of "AcpA"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fabG]]'', ''[[rnc]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fabG]]'', ''[[rnc]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15920 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15920 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15920 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15920 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15920 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15920 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:acpA_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:acpA_context.gif]]

Revision as of 10:12, 14 May 2013

  • 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
Sequences Protein DNA DNA_with_flanks
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

Max J Cryle
Selectivity in a barren landscape: the P450(BioI)-ACP complex.
Biochem Soc Trans: 2010, 38(4);934-9
[PubMed:20658980] [WorldCat.org] [DOI] (I p)

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

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)