TepA

• Description: sporulation protein, signal peptide peptidase required for efficient processing of pre-proteins
  
  

Gene name	tepA
Synonyms	ymfB, ylxI
Essential	no
Product	signal peptide peptidase
Function	protein secretion
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein secretion, sporulation proteins

This gene is a member of the following regulons

SigG regulon

The gene

Basic information

• Locus tag: BSU16790

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• 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:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: Q99171

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: tepA-ylzJ PubMed

• Expression browser: tepA PubMed

• Sigma factor: SigG PubMed

• Regulation:
  • expressed late during sporulation in the forespore (SigG) PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP1120 (spc), available in the Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)