Difference between revisions of "FabG"
| Line 96: | Line 96: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
** induced if the cells experience an accumulation of malonyl-CoA ([[FapR]]) {{PubMed|12737802}} | ** induced if the cells experience an accumulation of malonyl-CoA ([[FapR]]) {{PubMed|12737802}} | ||
| + | ** expressed at high cell density ([[ComA]]) {{PubMed|16091051}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[ComA]]: transcription activation ([[ComA]]) {{PubMed|16091051}} | ||
** [[FapR]]: transcription repression {{PubMed|12737802}} | ** [[FapR]]: transcription repression {{PubMed|12737802}} | ||
| Line 124: | Line 126: | ||
<pubmed> 15952903 17919287</pubmed> | <pubmed> 15952903 17919287</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| − | <pubmed>12737802, 16932747 19850612 11669613 </pubmed> | + | <pubmed>12737802, 16932747 19850612 11669613 16091051</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 20:15, 15 February 2010
- Description: beta-ketoacyl-acyl carrier protein reductase
| Gene name | fabG |
| Synonyms | ylpF |
| Essential | yes PubMed |
| Product | beta-ketoacyl-acyl carrier protein reductase |
| Function | fatty acid biosynthesis |
| MW, pI | 26 kDa, 8.091 |
| Gene length, protein length | 738 bp, 246 aa |
| Immediate neighbours | fabD, acpA |
| 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: BSU15910
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH (according to Swiss-Prot)
- Protein family: short-chain dehydrogenases/reductases (SDR) family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: P51831
- KEGG entry: [3]
- E.C. number: 1.1.1.100
Additional information
Expression and regulation
- 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
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, Marcelo Guerin, Alejandro Buschiazzo, Francis Schaeffer, Leticia I Llarrull, Georgina Reh, Alejandro J Vila, Pedro M Alzari, Diego de Mendoza
Structural basis of lipid biosynthesis regulation in Gram-positive bacteria.
EMBO J: 2006, 25(17);4074-83
[PubMed:16932747]
[WorldCat.org]
[DOI]
(P p)
Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051]
[WorldCat.org]
[DOI]
(P 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)
A C Price, Y M Zhang, C O Rock, S W White
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Biochemistry: 2001, 40(43);12772-81
[PubMed:11669613]
[WorldCat.org]
[DOI]
(P p)
