Difference between revisions of "LcfA"
| Line 104: | Line 104: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| − | ** | + | ** subject to carbon catabolite repression ([[CcpA]]-[[PtsH|HPr(Ser-P)]] {{PubMed|21398533}} |
** induced by long chain acyl-CoA (C14 ... C20) ([[FadR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/17189250 PubMed] | ** induced by long chain acyl-CoA (C14 ... C20) ([[FadR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/17189250 PubMed] | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | ** [[CcpA]]: transcription repression | + | ** [[CcpA]]-[[PtsH|HPr(Ser-P)]]: transcription repression {{PubMed|21398533}} |
** [[FadR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/17189250 PubMed] | ** [[FadR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/17189250 PubMed] | ||
| Line 133: | Line 133: | ||
=References= | =References= | ||
| − | + | '''Additional publications:''' {{PubMed|21398533}} | |
<pubmed>17189250,17919287 20797616 17085570 </pubmed> | <pubmed>17189250,17919287 20797616 17085570 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:52, 19 March 2011
- Description: long chain acyl-CoA synthetase, involved in surfactin production
| Gene name | lcfA |
| Synonyms | |
| Essential | no |
| Product | long chain acyl-CoA synthetase |
| Function | fatty acid degradation |
| Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
| MW, pI | 62 kDa, 6.119 |
| Gene length, protein length | 1680 bp, 560 aa |
| Immediate neighbours | fadR, yshE |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28560
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA (according to Swiss-Prot), activates 3-hydroxy fatty acids for surfactin biosynthesis PubMed
- Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P94547
- KEGG entry: [3]
- E.C. number: 6.2.1.3
Additional information
Expression and regulation
- Regulation:
- subject to carbon catabolite repression (CcpA-HPr(Ser-P) PubMed
- induced by long chain acyl-CoA (C14 ... C20) (FadR) PubMed
- Regulatory mechanism:
- CcpA-HPr(Ser-P): transcription repression PubMed
- FadR: transcription repression PubMed
- Additional information:
Biological materials
- Mutant: available in Mohamed Marahiel's lab PubMed
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
Femke I Kraas, Verena Helmetag, Melanie Wittmann, Matthias Strieker, Mohamed A Marahiel
Functional dissection of surfactin synthetase initiation module reveals insights into the mechanism of lipoinitiation.
Chem Biol: 2010, 17(8);872-80
[PubMed:20797616]
[WorldCat.org]
[DOI]
(I p)
Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287]
[WorldCat.org]
[DOI]
(P p)
Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation.
J Biol Chem: 2007, 282(8);5180-94
[PubMed:17189250]
[WorldCat.org]
[DOI]
(P p)
Chiara Barabesi, Alessandro Galizzi, Giorgio Mastromei, Mila Rossi, Elena Tamburini, Brunella Perito
Bacillus subtilis gene cluster involved in calcium carbonate biomineralization.
J Bacteriol: 2007, 189(1);228-35
[PubMed:17085570]
[WorldCat.org]
[DOI]
(P p)
