Difference between revisions of "HtrA"
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34358 O34358] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34358 O34358] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU12900] |
* '''E.C. number:''' | * '''E.C. number:''' |
Revision as of 02:43, 25 June 2009
- Description: serine protease Do (heat-shock protein)
Gene name | htrA |
Synonyms | ykdA |
Essential | no |
Product | serine protease Do (heat-shock protein) |
Function | probably involved in processing, maturation, or secretion of extracellular enzymes |
Metabolic function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 47 kDa, 4.699 |
Gene length, protein length | 1347 bp, 449 aa |
Immediate neighbours | ykcC, proG |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
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): YyxA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot), extracellular (signal peptide) PubMed
Database entries
- Structure:
- Swiss prot entry: O34358
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
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)
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)