Difference between revisions of "LipA"

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|style="background:#ABCDEF;" align="center"|'''Function''' || lipid metabolism, required for the synthesis of branched-chain amino acids  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || lipid metabolism, required for the synthesis of branched-chain amino acids  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU32330 lipA]
 
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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/wiki/index.php/Protein_secretion Protein secretion]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]'''

Revision as of 15:37, 7 August 2012

  • Description: trigger enzyme: lipoic acid synthase and regulator of comE operon expression

Gene name lipA
Synonyms yutB
Essential Yes PubMed
Product trigger enzyme: lipoic acid synthase
Function lipid metabolism, required for the synthesis of branched-chain amino acids
Gene expression levels in SubtiExpress: lipA
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 33 kDa, 8.251
Gene length, protein length 894 bp, 298 aa
Immediate neighbours yutC, lytH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LipA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LipA expression.png
























Categories containing this gene/protein

biosynthesis of cofactors, trigger enzyme

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU32330

Phenotypes of a mutant

reduced transformation efficiency PubMed, strong inhibition of growth on minimal media PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine (according to Swiss-Prot) Triacylglycerol + H2O = diacylglycerol + a carboxylate (according to Swiss-Prot) required for comEA transcription PubMed
  • Protein family: Lipoyl synthase family (according to Swiss-Prot) AB hydrolase superfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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

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)

Mitsuo Ogura, Teruo Tanaka
The Bacillus subtilis late competence operon comE is transcriptionally regulated by yutB and under post-transcription initiation control by comN (yrzD).
J Bacteriol: 2009, 191(3);949-58
[PubMed:19028902] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)