TepA

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  • Description: orphan ClpP-like germination protease, contributes to SASP degradation

Gene name tepA
Synonyms ymfB, ylxI
Essential no
Product germination protease
Function degradation of SASPs
Gene expression levels in SubtiExpress: tepA
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 24 kDa, 5.575
Gene length, protein length 669 bp, 223 aa
Immediate neighbours rnjB, ylzJ
Sequences Protein DNA DNA_with_flanks
Genetic context
TepA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TepA expression.png















Categories containing this gene/protein

proteolysis, germination

This gene is a member of the following regulons

SigG regulon, SpoVT regulon,

The gene

Basic information

  • Locus tag: BSU16790

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • degradation of SASPs in germinating spores PubMed
  • Protein family: TepA subfamily (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:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP1120 (spc), available in the Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Bjorn A Traag, Antonia Pugliese, Barbara Setlow, Peter Setlow, Richard Losick
A conserved ClpP-like protease involved in spore outgrowth in Bacillus subtilis.
Mol Microbiol: 2013, 90(1);160-6
[PubMed:23927687] [WorldCat.org] [DOI] (I p)

Bjorn A Traag, Antonia Pugliese, Jonathan A Eisen, Richard Losick
Gene conservation among endospore-forming bacteria reveals additional sporulation genes in Bacillus subtilis.
J Bacteriol: 2013, 195(2);253-60
[PubMed:23123912] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

A Bolhuis, A Matzen, H L Hyyryläinen, V P Kontinen, R Meima, J Chapuis, G Venema, S Bron, R Freudl, J M van Dijl
Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins.
J Biol Chem: 1999, 274(35);24585-92
[PubMed:10455123] [WorldCat.org] [DOI] (P p)