Difference between revisions of "WapA"

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* '''Additional information:'''
 
* '''Additional information:'''
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 66 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 6 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 51 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:16, 17 April 2014

  • Description: cell wall-associated protein precursor, contact-dependent growth inhibition protein

Gene name wapA
Synonyms
Essential no
Product cell wall-associated protein precursor
Function intercellular competition
Gene expression levels in SubtiExpress: wapA
Interactions involving this protein in SubtInteract: WapA
MW, pI 258 kDa, 6.131
Gene length, protein length 7002 bp, 2334 aa
Immediate neighbours yxxG, yxxF
Sequences Protein DNA DNA_with_flanks
Genetic context
WapA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
WapA expression.png















Categories containing this gene/protein

cell wall/ other, toxins, antitoxins and immunity against toxins

This gene is a member of the following regulons

DegU regulon, WalR regulon, YvrHb regulon

The gene

Basic information

  • Locus tag: BSU39230

Phenotypes of a mutant

Database entries

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

Additional information

  • A mutation was found in this gene after evolution under relexed selection for sporulation PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • the C-terminal toxic domain has RNase activity (cleaves tRNAs) PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • cell wall binding domain as retention signal
    • C-terminal toxic domain with RNase activity (cleaves tRNAs) PubMed
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • extracellular (signal peptide), cell wall binding domain as retention signal, major constituent of the secretome PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • repressed at high salt concentration (DegU-P) PubMed
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 66 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 6 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 51 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Sanna Koskiniemi, James G Lamoureux, Kiel C Nikolakakis, Claire t'Kint de Roodenbeke, Michael D Kaplan, David A Low, Christopher S Hayes
Rhs proteins from diverse bacteria mediate intercellular competition.
Proc Natl Acad Sci U S A: 2013, 110(17);7032-7
[PubMed:23572593] [WorldCat.org] [DOI] (I p)

Letal I Salzberg, Leagh Powell, Karsten Hokamp, Eric Botella, David Noone, Kevin M Devine
The WalRK (YycFG) and σ(I) RsgI regulators cooperate to control CwlO and LytE expression in exponentially growing and stressed Bacillus subtilis cells.
Mol Microbiol: 2013, 87(1);180-95
[PubMed:23199363] [WorldCat.org] [DOI] (I p)

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [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)

Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann
Role of the Fur regulon in iron transport in Bacillus subtilis.
J Bacteriol: 2006, 188(10);3664-73
[PubMed:16672620] [WorldCat.org] [DOI] (P 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)

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)

V Dartois, M Débarbouillé, F Kunst, G Rapoport
Characterization of a novel member of the DegS-DegU regulon affected by salt stress in Bacillus subtilis.
J Bacteriol: 1998, 180(7);1855-61
[PubMed:9537385] [WorldCat.org] [DOI] (P p)