AcpA
-  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  
  This image was kindly provided by SubtiList 
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Contents
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
- UniProt: P80643
 
- KEGG entry: [2]
 
- E.C. number:
 
Additional information
Expression and regulation
- 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
 
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)
