Difference between revisions of "LcfA"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28560 lcfA]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28560 lcfA]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_deg.html Fatty acid degradation]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=lcfA lcfA]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 62 kDa, 6.119   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 62 kDa, 6.119   

Revision as of 11:24, 7 January 2014

  • 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
Gene expression levels in SubtiExpress: lcfA
Metabolic function and regulation of this protein in SubtiPathways:
lcfA
MW, pI 62 kDa, 6.119
Gene length, protein length 1680 bp, 560 aa
Immediate neighbours fadR, yshE
Sequences Protein DNA DNA_with_flanks
Genetic context
LcfA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LcfA expression.png




























Categories containing this gene/protein

utilization of lipids

This gene is a member of the following regulons

CcpA regulon, FadR regulon

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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

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)