Difference between revisions of "HtrA"

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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=htrA_1357936_1359285_-1 htrA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=htrA_1357936_1359285_-1 htrA] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigA]] {{PubMed|10692364}}
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* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|10692364}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Additional information:'''
 
* '''Additional information:'''
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** [[HtrA]] is subject to degradation by [[WprA]] and other extracellular proteases {{PubMed|24362423}}
  
 
=Biological materials =
 
=Biological materials =
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== Original publications ==
 
== Original publications ==
<pubmed>17600057,12270824 ,11555295,18957862, 10692364 21624103 22307758 22092710</pubmed>
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<pubmed>17600057,12270824 ,11555295,18957862, 10692364 21624103 22307758 22092710 24362423</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:29, 16 January 2014

  • Description: membrane-anchored protein quality control protease, serine protease Do

Gene name htrA
Synonyms ykdA
Essential no
Product serine protease Do
Function protein quality control
Gene expression levels in SubtiExpress: htrA
Metabolic function and regulation of this protein in SubtiPathways:
htrA
MW, pI 47 kDa, 4.699
Gene length, protein length 1347 bp, 449 aa
Immediate neighbours ykcC, proG
Sequences Protein DNA DNA_with_flanks
Genetic context
HtrA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HtrA expression.png















Categories containing this gene/protein

proteolysis, heat shock proteins, membrane proteins

This gene is a member of the following regulons

CssR regulon

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): HtrC

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • cell membrane (according to Swiss-Prot)
    • extracellular (signal peptide) PubMed
    • randomly distributed in foci throughout the cell surface PubMed

Database entries

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

Additional information

Expression and regulation

  • Operon: htrA (according to DBTBS)
  • Regulation:
    • expressed under conditions of secretion stress (CssR) PubMed
    • induced by rhamnolipids PubMed
  • Regulatory mechanism:
  • Additional information:
    • HtrA is subject to degradation by WprA and other extracellular proteases PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Ross E Dalbey, Peng Wang, Jan Maarten van Dijl
Membrane proteases in the bacterial protein secretion and quality control pathway.
Microbiol Mol Biol Rev: 2012, 76(2);311-30
[PubMed:22688815] [WorldCat.org] [DOI] (I p)

Tim Clausen, Markus Kaiser, Robert Huber, Michael Ehrmann
HTRA proteases: regulated proteolysis in protein quality control.
Nat Rev Mol Cell Biol: 2011, 12(3);152-62
[PubMed:21326199] [WorldCat.org] [DOI] (I p)


Original publications

Laxmi Krishnappa, Carmine G Monteferrante, Jolanda Neef, Annette Dreisbach, Jan Maarten van Dijl
Degradation of extracytoplasmic catalysts for protein folding in Bacillus subtilis.
Appl Environ Microbiol: 2014, 80(4);1463-8
[PubMed:24362423] [WorldCat.org] [DOI] (I p)

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)

Tina Wecke, Tobias Bauer, Henning Harth, Ulrike Mäder, Thorsten Mascher
The rhamnolipid stress response of Bacillus subtilis.
FEMS Microbiol Lett: 2011, 323(2);113-23
[PubMed:22092710] [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)