HtrA

• 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

The gene

Basic information

• Locus tag: BSU12900

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• UniProt: O34358

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

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

• Regulatory mechanism:
  • CssR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)