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]]'' | ||
|- | |- | ||
− | |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 | + | |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] |
|- | |- | ||
|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 ![]() This image was kindly provided by SubtiList
| |
Expression at a glance PubMed![]() |
Contents
Categories containing this gene/protein
biosynthesis of lipids, essential genes
This gene is a member of the following regulons
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
- 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
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)