HtrA

• Description: serine protease Do
  
  

Gene name	htrA
Synonyms	ykdA
Essential	no
Product	serine protease Do
Function	probably involved in processing, maturation, or secretion of extracellular enzymes
Gene expression levels in SubtiExpress: htrA
Metabolic function and regulation of this protein in SubtiPathways: Stress, Protein secretion
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
Expression at a glance   PubMed

Categories containing this gene/protein

proteolysis, heat shock proteins

This gene is a member of the following regulons

CssR regulon

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
  • randomly distributed in foci throughout the cell surface PubMed

Database entries

• Structure:

• UniProt: O34358

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: htrA (according to DBTBS)

• Expression browser: htrA PubMed

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • CssR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Hein Trip, Patricia J van der Veek, Ton C Renniers, Rob Meima, Cees M Sagt, Lisette Mohrmann, Oscar P Kuipers
A novel screening system for secretion of heterologous proteins in Bacillus subtilis.
Microb Biotechnol: 2011, 4(5);673-82
[PubMed:21624103] [WorldCat.org] [DOI] (I p)

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)

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)

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)

D Noone, A Howell, K M Devine
Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated.
J Bacteriol: 2000, 182(6);1592-9
[PubMed:10692364] [WorldCat.org] [DOI] (P p)