AcpA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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:

• Interactions:
  • AcpA-AcpS PubMed
  • AcpA-BioI PubMed
  • malonyl-ACP-FapR PubMed

• Localization: cytoplasm (according to Swiss-Prot), during sporulation in the mother cell PubMed

Database entries

• Structure: 1F80 (complex with AcpS) PubMed, 3EJE (complex with BioI) PubMed, 1HY8

• UniProt: P80643

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:
  • fapR-plsX-fabD-fabG-acpA PubMed
  • acpA PubMed

• Expression browser: acpA PubMed

• Sigma factor:
  • fapR: SigA PubMed

• 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:
  • FapR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Diego de Mendoza, Universidad Nacional de Rosario, Argentine homepage

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)