Difference between revisions of "HtrB"
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Revision as of 14:31, 16 May 2013
- Description: membrane-anchored protein quality control protease, serine protease, response to secretion and heat stresses
| Gene name | htrB |
| Synonyms | yvtA, yvtB |
| Essential | no |
| Product | serine protease |
| Function | protein quality control |
| Gene expression levels in SubtiExpress: htrB | |
| Metabolic function and regulation of this protein in SubtiPathways: Stress, Protein secretion | |
| MW, pI | 48 kDa, 4.632 |
| Gene length, protein length | 1374 bp, 458 aa |
| Immediate neighbours | mrgA, cssR |
| 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: BSU33000
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: peptidase S1B 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)
- randomly distributed in foci throughout the cell surface PubMed
Database entries
- Structure:
- UniProt: Q9R9I1
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: htrB (according to DBTBS)
- 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
Additional publications: PubMed
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)
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)
