Difference between revisions of "TepA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || [[protein secretion]] | |style="background:#ABCDEF;" align="center"|'''Function''' || [[protein secretion]] | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU16790 tepA] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | ||
| Line 24: | Line 24: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rnjB]]'', ''[[ylzJ]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rnjB]]'', ''[[ylzJ]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU16790 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU16790 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU16790 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:tepA_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:tepA_context.gif]] | ||
Revision as of 12:52, 13 May 2013
- 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 Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
protein secretion, sporulation proteins
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:
- 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:
- 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) 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:
Labs working on this gene/protein
Your additional remarks
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)
