Difference between revisions of "HtpX"
| Line 105: | Line 105: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[ykrL]]'' {{PubMed|22383849}} |
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=htpX_1414997_1415893_1 ykrL] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=htpX_1414997_1415893_1 ykrL] {{PubMed|22383849}} | ||
| Line 112: | Line 112: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| − | ** induced by membrane protein overproduction ([[YkrK]]) {{PubMed|22447908}} | + | ** induced by membrane protein overproduction ([[YkrK]]) {{PubMed|22624725,22447908}} |
** induced by dissipation of membrane potential (ΔΨ) by addition of a sublethal concentration of valinomycin {{PubMed|22447908}} | ** induced by dissipation of membrane potential (ΔΨ) by addition of a sublethal concentration of valinomycin {{PubMed|22447908}} | ||
** expression is increased due to mutations in ''[[resE]]'', ''[[resB]]'', ''[[sdhC]]'', and'' [[sdhA]]'' {{PubMed|22447908}} | ** expression is increased due to mutations in ''[[resE]]'', ''[[resB]]'', ''[[sdhC]]'', and'' [[sdhA]]'' {{PubMed|22447908}} | ||
| Line 142: | Line 142: | ||
=References= | =References= | ||
| − | <pubmed> 22447908 </pubmed> | + | <pubmed> 22447908 22624725 22383849</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 14:56, 4 June 2012
- Description: similar to E.coli HtpX heat shock protease, stress-responsive membrane protease
| Gene name | ykrL |
| Synonyms | htpX |
| Essential | no |
| Product | membrane protease |
| Function | quality control of membrane proteins |
| MW, pI | 32 kDa, 10.157 |
| Gene length, protein length | 894 bp, 298 aa |
| Immediate neighbours | ykrK, ktrD |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
membrane proteins, proteolysis
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13490
Phenotypes of a mutant
- increased sensitivity to membrane protein overproduction PubMed
- increased sensitivity to dissipation of the membrane potential by the addition of valinomycin PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: peptidase M48B family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O31657
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Bogumiła C Marciniak, Hein Trip, Patricia J van-der Veek, Oscar P Kuipers
Comparative transcriptional analysis of Bacillus subtilis cells overproducing either secreted proteins, lipoproteins or membrane proteins.
Microb Cell Fact: 2012, 11;66
[PubMed:22624725]
[WorldCat.org]
[DOI]
(I e)
Bogumila C Marciniak, Hein Trip, Fabrizia Fusetti, Oscar P Kuipers
Regulation of ykrL (htpX) by Rok and YkrK, a novel type of regulator in Bacillus subtilis.
J Bacteriol: 2012, 194(11);2837-45
[PubMed:22447908]
[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)
