Difference between revisions of "WprA"

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(References)
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=References=
 
=References=
<pubmed> 22900538 22923395 23180473</pubmed>
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<pubmed> 22900538 22923395 23180473 21815947 10075409,11987133,9004506,20525796,18957862 18763711 16306698, 9687444 12028417 </pubmed>
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
 
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
 
<big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
<pubmed>10075409,11987133,9004506,20525796,18957862 18763711 16306698, 9687444 12028417 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:18, 13 July 2013

  • Description: secreted quality control protease

Gene name wprA
Synonyms yisM
Essential no
Product secreted quality control protease
Function protein quality control
Gene expression levels in SubtiExpress: wprA
Interactions involving this protein in SubtInteract: WprA
MW, pI 96 kDa, 9.58
Gene length, protein length 2682 bp, 894 aa
Immediate neighbours yisL, yisN
Sequences Protein DNA DNA_with_flanks
Genetic context
WprA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
WprA expression.png















Categories containing this gene/protein

cell wall/ other, proteolysis,

This gene is a member of the following regulons

YvrHb regulon, CcpA regulon

The gene

Basic information

  • Locus tag: BSU10770

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Protein family: peptidase S8 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Carmine G Monteferrante, Calum MacKichan, Elodie Marchadier, Maria-Victoria Prejean, Rut Carballido-López, Jan Maarten van Dijl
Mapping the twin-arginine protein translocation network of Bacillus subtilis.
Proteomics: 2013, 13(5);800-11
[PubMed:23180473] [WorldCat.org] [DOI] (I p)

Laxmi Krishnappa, Carmine G Monteferrante, Jan Maarten van Dijl
Degradation of the twin-arginine translocation substrate YwbN by extracytoplasmic proteases of Bacillus subtilis.
Appl Environ Microbiol: 2012, 78(21);7801-4
[PubMed:22923395] [WorldCat.org] [DOI] (I p)

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Masakuni Serizawa, Keisuke Kodama, Hiroki Yamamoto, Kazuo Kobayashi, Naotake Ogasawara, Junichi Sekiguchi
Functional analysis of the YvrGHb two-component system of Bacillus subtilis: identification of the regulated genes by DNA microarray and northern blot analyses.
Biosci Biotechnol Biochem: 2005, 69(11);2155-69
[PubMed:16306698] [WorldCat.org] [DOI] (P p)

K Stephenson, C L Jensen, S T Jørgensen, C R Harwood
Simultaneous inactivation of the wprA and dltB genes of Bacillus subtilis reduces the yield of alpha-amylase.
Lett Appl Microbiol: 2002, 34(6);394-7
[PubMed:12028417] [WorldCat.org] [DOI] (P p)

Haike Antelmann, Hiroki Yamamoto, Junichi Sekiguchi, Michael Hecker
Stabilization of cell wall proteins in Bacillus subtilis: a proteomic approach.
Proteomics: 2002, 2(5);591-602
[PubMed:11987133] [WorldCat.org] [DOI] (P p)

J H Hageman, R L Switzer
ISP-4 and CWBP52 are proteins encoded by the same gene in Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 2);281
[PubMed:10075409] [WorldCat.org] [DOI] (P p)

K Stephenson, C R Harwood
Influence of a cell-wall-associated protease on production of alpha-amylase by Bacillus subtilis.
Appl Environ Microbiol: 1998, 64(8);2875-81
[PubMed:9687444] [WorldCat.org] [DOI] (P p)

P Margot, D Karamata
The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease.
Microbiology (Reading): 1996, 142 ( Pt 12);3437-44
[PubMed:9004506] [WorldCat.org] [DOI] (P p)