Difference between revisions of "HtrA"
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=htrA_1357936_1359285_-1 htrA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=htrA_1357936_1359285_-1 htrA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|10692364}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|10692364}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** [[HtrA]] is subject to degradation by [[WprA]] and other extracellular proteases {{PubMed|24362423}} | ||
=Biological materials = | =Biological materials = | ||
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== Original publications == | == Original publications == | ||
| − | <pubmed>17600057,12270824 ,11555295,18957862, 10692364 21624103 22307758 22092710</pubmed> | + | <pubmed>17600057,12270824 ,11555295,18957862, 10692364 21624103 22307758 22092710 24362423</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:29, 16 January 2014
- Description: membrane-anchored protein quality control protease, serine protease Do
| Gene name | htrA |
| Synonyms | ykdA |
| Essential | no |
| Product | serine protease Do |
| Function | protein quality control |
| Gene expression levels in SubtiExpress: htrA | |
| Metabolic function and regulation of this protein in SubtiPathways: htrA | |
| MW, pI | 47 kDa, 4.699 |
| Gene length, protein length | 1347 bp, 449 aa |
| Immediate neighbours | ykcC, proG |
| 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
proteolysis, heat shock proteins, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU12900
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: PDZ (DHR) domain (according to Swiss-Prot)
- Paralogous protein(s): HtrC
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O34358
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: htrA (according to DBTBS)
- Regulation:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications
Laxmi Krishnappa, Carmine G Monteferrante, Jolanda Neef, Annette Dreisbach, Jan Maarten van Dijl
Degradation of extracytoplasmic catalysts for protein folding in Bacillus subtilis.
Appl Environ Microbiol: 2014, 80(4);1463-8
[PubMed:24362423]
[WorldCat.org]
[DOI]
(I p)
David Noone, Eric Botella, Clodagh Butler, Annette Hansen, Inga Jende, Kevin M Devine
Signal perception by the secretion stress-responsive CssRS two-component system in Bacillus subtilis.
J Bacteriol: 2012, 194(7);1800-14
[PubMed:22307758]
[WorldCat.org]
[DOI]
(I p)
Tina Wecke, Tobias Bauer, Henning Harth, Ulrike Mäder, Thorsten Mascher
The rhamnolipid stress response of Bacillus subtilis.
FEMS Microbiol Lett: 2011, 323(2);113-23
[PubMed:22092710]
[WorldCat.org]
[DOI]
(I p)
Hein Trip, Patricia J van der Veek, Ton C Renniers, Rob Meima, Cees M Sagt, Lisette Mohrmann, Oscar P Kuipers
A novel screening system for secretion of heterologous proteins in Bacillus subtilis.
Microb Biotechnol: 2011, 4(5);673-82
[PubMed:21624103]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Hanne-Leena Hyyryläinen, Milla Pietiäinen, Tuula Lundén, Anna Ekman, Marika Gardemeister, Sanna Murtomäki-Repo, Haike Antelmann, Michael Hecker, Leena Valmu, Matti Sarvas, Vesa P Kontinen
The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 7);2126-2136
[PubMed:17600057]
[WorldCat.org]
[DOI]
(P p)
Elise Darmon, David Noone, Anne Masson, Sierd Bron, Oscar P Kuipers, Kevin M Devine, Jan Maarten van Dijl
A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis.
J Bacteriol: 2002, 184(20);5661-71
[PubMed:12270824]
[WorldCat.org]
[DOI]
(P p)
H L Hyyryläinen, A Bolhuis, E Darmon, L Muukkonen, P Koski, M Vitikainen, M Sarvas, Z Prágai, S Bron, J M van Dijl, V P Kontinen
A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress.
Mol Microbiol: 2001, 41(5);1159-72
[PubMed:11555295]
[WorldCat.org]
[DOI]
(P p)
D Noone, A Howell, K M Devine
Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated.
J Bacteriol: 2000, 182(6);1592-9
[PubMed:10692364]
[WorldCat.org]
[DOI]
(P p)
