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+BSU12900]
+
* '''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
HtrA context.gif
This image was kindly provided by SubtiList







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:
  • 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

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)