LplJ

From SubtiWiki
Jump to: navigation, search

SubtiWiki goes mobile!

Do you want to check genes or proteins wherever you are? Want to takes private notes and add your ideas and pictures to your favorite genes?

Then go and download the new SubtiWiki app, which is available for iOS and Android devices!

Enjoy it!

Download on the App store Get it on Google Play

  • 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

Contents
























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
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 274 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 330 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 360 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)

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox