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: acpA
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 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

• BsubCyc: BSU15920

• 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

• BsubCyc: BSU15920

• 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

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

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)