Difference between revisions of "Lip"

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* '''Operon:''' ''[[lip]]'' {{PubMed|21815947}}
  
* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=estA_292205_292843_1 lip] {{PubMed|22383849}}
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Revision as of 15:17, 7 August 2012

  • Description: extracellular lipase

Gene name lip
Synonyms lipA
Essential no
Product extracellular lipase
Function lipid degradation
MW, pI 22 kDa, 10.059
Gene length, protein length 636 bp, 212 aa
Immediate neighbours ansZ, yczC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Lip context.gif
This image was kindly provided by SubtiList




Categories containing this gene/protein

utilization of lipids

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

  • Locus tag: BSU02700

Expression

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Wojciech Augustyniak, Agnieszka A Brzezinska, Tjaard Pijning, Hans Wienk, Rolf Boelens, Bauke W Dijkstra, Manfred T Reetz
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.
Protein Sci: 2012, 21(4);487-97
[PubMed:22267088] [WorldCat.org] [DOI] (I p)

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947