Difference between revisions of "TepA"
| Line 1: | Line 1: | ||
| − | * '''Description:''' [[germination]] protease, | + | * '''Description:''' orphan ClpP-like [[germination]] protease, contributes to SASP degradation<br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 40: | Line 40: | ||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | {{SubtiWiki category|[[ | + | {{SubtiWiki category|[[proteolysis]]}}, |
| − | {{SubtiWiki category|[[ | + | {{SubtiWiki category|[[germination]]}} |
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | {{SubtiWiki regulon|[[SigG regulon]]}} | + | {{SubtiWiki regulon|[[SigG regulon]]}}, |
| + | {{SubtiWiki regulon|[[SpoVT regulon]]}}, | ||
=The gene= | =The gene= | ||
| Line 70: | Line 71: | ||
* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
| + | ** degradation of SASPs in germinating spores {{PubMed|23927687}} | ||
* '''Protein family:''' TepA subfamily (according to Swiss-Prot) | * '''Protein family:''' TepA subfamily (according to Swiss-Prot) | ||
| Line 86: | Line 88: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| + | ** activity requires [[YlzJ]] {{PubMed|23927687}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
| Line 113: | Line 116: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| − | ** expressed late during [[sporulation]] in the forespore ([[SigG]]) {{PubMed|23123912}} | + | ** expressed late during [[sporulation]] in the forespore ([[SigG]], [[SpoVT]]) {{PubMed|23123912}} |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[SpoVT]]: transcription repression {{PubMed|23123912}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Revision as of 14:32, 12 August 2013
- 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
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):
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: Q99171
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- expressed late during sporulation in the forespore (SigG, SpoVT) PubMed
- 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)
