HtrC

• Description: similar to quality control membrane serine protease HtrA
  
  

Gene name	htrC
Synonyms	yycK, yyxA
Essential	no
Product	putative quality control membrane protease
Function	unknown
Gene expression levels in SubtiExpress: htrC
MW, pI	42 kDa, 5.315
Gene length, protein length	1200 bp, 400 aa
Immediate neighbours	yyzO, walJ
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

proteolysis, sporulation proteins, membrane proteins

This gene is a member of the following regulons

SigG regulon

The gene

Basic information

• Locus tag: BSU40360

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: peptidase S1B family (according to Swiss-Prot)

• Paralogous protein(s): HtrA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • HtrC is a member of a suspected group of hubs proteins that were suggested to be involved in a large number of interactions PubMed

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

Database entries

• Structure:

• UniProt: P39668

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • walR-walK-yycH-yycI-walJ-htrC PubMed
  • yyxA PubMed

• Expression browser: htrC PubMed

• Sigma factor: for htrC: SigG PubMed

• Regulation:
  • expressed during vegetative growth, repressed during stationary phase PubMed
  • htrC transcript expressed during sporulation PubMed
  • walR-walK-yycH-yycI-walJ-htrC is induced upon deletion of htrA and htrB PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

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)

Susanne Pohl, Gaurav Bhavsar, Joanne Hulme, Alexandra E Bloor, Goksel Misirli, Matthew W Leckenby, David S Radford, Wendy Smith, Anil Wipat, E Diane Williamson, Colin R Harwood, Rocky M Cranenburgh
Proteomic analysis of Bacillus subtilis strains engineered for improved production of heterologous proteins.
Proteomics: 2013, 13(22);3298-308
[PubMed:24115457] [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)

Elodie Marchadier, Rut Carballido-López, Sophie Brinster, Céline Fabret, Peggy Mervelet, Philippe Bessières, Marie-Françoise Noirot-Gros, Vincent Fromion, Philippe Noirot
An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach.
Proteomics: 2011, 11(15);2981-91
[PubMed:21630458] [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)

C Fabret, J A Hoch
A two-component signal transduction system essential for growth of Bacillus subtilis: implications for anti-infective therapy.
J Bacteriol: 1998, 180(23);6375-83
[PubMed:9829949] [WorldCat.org] [DOI] (P p)