WprA

• 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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • important for TatAY-TatCY-dependent export of YkuE and YwbN PubMed

• 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:

• Interactions:
  • WprA-TatAY PubMed
  • WprA-TatCY PubMed

• Localization:
  • extracellular (signal peptide) PubMed
  • membrane PubMed
  • cell wall PubMed

Database entries

• Structure:

• UniProt: P54423

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: wprA PubMed

• Expression browser: wprA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • YvrHb: transcription activation PubMed

• Additional information:
  • An antisense RNA is predicted forwprA PubMed
  • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

• Mutant:
  • 1A1021 ( wprA::kan), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

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)