Difference between revisions of "LplJ"

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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 150 {{PubMed|24696501}}
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** number of protein molecules per cell (complex medium with amino acids, without glucose): 287 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 11:24, 17 April 2014

  • Description: lipoate-protein ligase

Gene name lplJ
Synonyms yhfJ
Essential no
Product Lipoate:protein ligase
Function lipoic acid metabolism
Gene expression levels in SubtiExpress: lplJ
Metabolic function and regulation of this protein in SubtiPathways:
LplJ
MW, pI 37 kDa, 5.835
Gene length, protein length 993 bp, 331 aa
Immediate neighbours yhfI, yhfK
Sequences Protein DNA DNA_with_flanks
Genetic context
YhfJ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LplJ expression.png
























Categories containing this gene/protein

Biosynthesis of cofactors

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU10250

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation: induced by valine PubMed
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 150 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 287 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Quin H Christensen, Natalia Martin, Maria C Mansilla, Diego de Mendoza, John E Cronan
A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis.
Mol Microbiol: 2011, 80(2);350-63
[PubMed:21338421] [WorldCat.org] [DOI] (I p)

Natalia Martin, Quin H Christensen, María C Mansilla, John E Cronan, Diego de Mendoza
A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis.
Mol Microbiol: 2011, 80(2);335-49
[PubMed:21338420] [WorldCat.org] [DOI] (I p)