Difference between revisions of "AcpA"
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1F80 1F80] (complex with AcpS), [http://www.rcsb.org/pdb/explore.do?structureId=3EJE 3EJE] (complex with BioI), [http://www.rcsb.org/pdb/explore.do?structureId=1HY8 1HY8] | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1F80 1F80] (complex with AcpS), [http://www.rcsb.org/pdb/explore.do?structureId=3EJE 3EJE] (complex with BioI), [http://www.rcsb.org/pdb/explore.do?structureId=1HY8 1HY8] | ||
− | * ''' | + | * '''UniProt:''' [http://www.uniprot.org/uniprot/P80643 P80643] |
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU15920] | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU15920] |
Revision as of 12:45, 20 July 2009
- 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
|
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)
Database entries
- UniProt: P80643
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- 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
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)