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
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

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
  • involved in degradation of PrsA, HtrA, and HtrB 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

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)

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)