HtrB

• Description: membrane-anchored protein quality control protease, serine protease, response to secretion and heat stresses
  
  

Gene name	htrB
Synonyms	yvtA, yvtB
Essential	no
Product	serine protease
Function	protein quality control
Gene expression levels in SubtiExpress: htrB
Metabolic function and regulation of this protein in SubtiPathways: htrB
MW, pI	48 kDa, 4.632
Gene length, protein length	1374 bp, 458 aa
Immediate neighbours	mrgA, cssR
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, heat shock proteins, membrane proteins

This gene is a member of the following regulons

CssR regulon

The gene

Basic information

• Locus tag: BSU33000

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):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:
  • cell membrane (according to Swiss-Prot)
  • randomly distributed in foci throughout the cell surface PubMed

Database entries

• Structure:

• UniProt: Q9R9I1

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: htrB (according to DBTBS)

• Expression browser: htrB PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • CssR: transcription activation PubMed

• Additional information:
  • HtrB is subject to degradation by WprA and other extracellular proteases PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)