Difference between revisions of "Proteolysis"

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(Genes in this functional category)
(Additional proteins involved in proteolysis)
 
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* ''[[htrA]]''
 
* ''[[htrA]]''
 
* ''[[htrB]]''
 
* ''[[htrB]]''
 +
* ''[[htrC]]''
 
* ''[[wprA]]''
 
* ''[[wprA]]''
  
=== Feeding proteases ===
+
=== Extracellular feeding proteases ===
 +
* [[AprE]] and [[NprE]] account for 95% of extracellular proteolytic activity
 +
 
 +
* ''[[aprE]]''
 
* ''[[bpr]]''
 
* ''[[bpr]]''
 
* ''[[epr]]''
 
* ''[[epr]]''
 
* ''[[mpr]]''
 
* ''[[mpr]]''
 
* ''[[nprB]]''
 
* ''[[nprB]]''
 +
* ''[[nprE]]''
 
* ''[[vpr]]''
 
* ''[[vpr]]''
 +
 +
* A mutant strain with deletions of all feeding proteases and the three major protein quality control proteases (''[[htrA]]'', ''[[htrB]]'', ''[[wprA]]'')  (BRB14) is available in [[Colin Harwood]]'s lab {{PubMed|24115457}}
  
 
=== Proteolysis during [[sporulation]]/ [[germination]] ===
 
=== Proteolysis during [[sporulation]]/ [[germination]] ===
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* ''[[mecA]]''
 
* ''[[mecA]]''
 
* ''[[mlpA]]''
 
* ''[[mlpA]]''
 +
* ''[[prp]]''
 
* ''[[prsW]]''
 
* ''[[prsW]]''
 
* ''[[rasP]]''
 
* ''[[rasP]]''
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* ''[[yqgP]]''
 
* ''[[yqgP]]''
 
* ''[[yraA]]''
 
* ''[[yraA]]''
 
== Additional candidates (based on similarity) ==
 
* ''[[yyxA]]''
 
  
 
== Important reviews ==
 
== Important reviews ==
<pubmed>19421188 23375660 23479438 22688815 </pubmed>
+
<pubmed>19421188 23375660 23479438 22688815 24099006 24115457</pubmed>
  
 
=Back to [[categories]]=
 
=Back to [[categories]]=

Latest revision as of 12:31, 10 December 2014

Parent categories
Neighbouring categories
Related categories

none

Genes in this functional category

Protein quality control

Extracellular feeding proteases

  • AprE and NprE account for 95% of extracellular proteolytic activity
  • A mutant strain with deletions of all feeding proteases and the three major protein quality control proteases (htrA, htrB, wprA) (BRB14) is available in Colin Harwood's lab PubMed

Proteolysis during sporulation/ germination

Additional proteins involved in proteolysis

Important reviews

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)

Lee Kroos, Yoshinori Akiyama
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
Biochim Biophys Acta: 2013, 1828(12);2873-85
[PubMed:24099006] [WorldCat.org] [DOI] (P p)

Noël Molière, Kürşad Turgay
General and regulatory proteolysis in Bacillus subtilis.
Subcell Biochem: 2013, 66;73-103
[PubMed:23479438] [WorldCat.org] [DOI] (P p)

Aurelia Battesti, Susan Gottesman
Roles of adaptor proteins in regulation of bacterial proteolysis.
Curr Opin Microbiol: 2013, 16(2);140-7
[PubMed:23375660] [WorldCat.org] [DOI] (I p)

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)

Sinisa Urban
Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms.
Nat Rev Microbiol: 2009, 7(6);411-23
[PubMed:19421188] [WorldCat.org] [DOI] (I p)


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