Difference between revisions of "HtrB"

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* '''Structure:'''
 
* '''Structure:'''
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/Q9R9I1 Q9R9I1]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/Q9R9I1 Q9R9I1]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU33000]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU33000]

Revision as of 14:28, 20 July 2009

  • Description: serine protease, response to secretion and heat stresses

Gene name htrB
Synonyms yvtA, yvtB
Essential no
Product serine protease
Function response to secretion and heat stresses
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 48 kDa, 4.632
Gene length, protein length 1374 bp, 458 aa
Immediate neighbours mrgA, cssR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvtA context.gif
This image was kindly provided by SubtiList







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:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • expressed under conditions of secretion stress (CssR) PubMed
  • Regulatory mechanism:
  • 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

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)