Difference between revisions of "FabHA"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fabHA_1208222_1209160_1 fabHA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fabHA_1208222_1209160_1 fabHA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|12737802}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|12737802}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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<pubmed> 15952903 17919287</pubmed> | <pubmed> 15952903 17919287</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| − | + | <pubmed>12737802,17114254,10629181, 10673437,19820084 21383089 21542858</pubmed> | |
| − | <pubmed>12737802,17114254,10629181, 10673437,19820084 21383089</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 15:30, 18 March 2014
- Description: beta-ketoacyl-acyl carrier protein synthase III, principal condensing enzyme responsible for the initiation of fatty acid synthesis in non-stressed B. subtilis cells
| Gene name | fabHA |
| Synonyms | yjaX , fabH1 |
| Essential | no |
| Product | beta-ketoacyl-acyl carrier protein synthase III |
| Function | fatty acid biosynthesis |
| Gene expression levels in SubtiExpress: fabHA | |
| Metabolic function and regulation of this protein in SubtiPathways: fabHA | |
| MW, pI | 33 kDa, 5.045 |
| Gene length, protein length | 936 bp, 312 aa |
| Immediate neighbours | yjzB, fabF |
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU11330
Phenotypes of a mutant
- significant increase in the proportion of straight-chain fatty acids with a concomitant increase in 31:0-carbon phosphatidylethanolamine species PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2 (according to Swiss-Prot)
- Protein family: fabH family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: O34746
- KEGG entry: [3]
Additional information
- affinity for butyryl-CoA, but prefers acetyl-CoA in fatty acid biosynthesis PubMed
Expression and regulation
- Regulation:
- expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
- inhibited by cerulenin PubMed
- induced upon fatty acid biosynthesis inhibition PubMed
- expression is reduced when SigW is activated (by alkaline shock, polymyxin B, vancomycin, cephalosporin C, D-cycloserine, and triton X-100) PubMed
- 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
Anthony W Kingston, Chitra Subramanian, Charles O Rock, John D Helmann
A σW-dependent stress response in Bacillus subtilis that reduces membrane fluidity.
Mol Microbiol: 2011, 81(1);69-79
[PubMed:21542858]
[WorldCat.org]
[DOI]
(I p)
Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089]
[WorldCat.org]
[DOI]
(I p)
Natalia Martin, Esteban Lombardía, Silvia G Altabe, Diego de Mendoza, María C Mansilla
A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis.
J Bacteriol: 2009, 191(24);7447-55
[PubMed:19820084]
[WorldCat.org]
[DOI]
(I p)
Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254]
[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)
C Davies, R J Heath, S W White, C O Rock
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Structure: 2000, 8(2);185-95
[PubMed:10673437]
[WorldCat.org]
[DOI]
(P p)
K H Choi, R J Heath, C O Rock
beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.
J Bacteriol: 2000, 182(2);365-70
[PubMed:10629181]
[WorldCat.org]
[DOI]
(P p)
