Difference between revisions of "PbpA"

From SubtiWiki
Jump to: navigation, search
Line 37: Line 37:
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
 
 
 
<br/><br/>
 
<br/><br/>
  
Line 112: Line 108:
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pbpA_2581771_2583921_-1 pbpA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pbpA_2581771_2583921_-1 pbpA] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 142: Line 138:
  
 
=References=
 
=References=
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
+
<pubmed>9851991,9139922,12896990 ,18957862, 20487272 21636744,21636745 21815947 </pubmed>
<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>9851991,9139922,12896990 ,18957862, 20487272 21636744,21636745</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 06:47, 4 June 2013

Gene name pbpA
Synonyms yqgF
Essential no
Product penicillin-binding protein PBP 2A
Function formation of a rod-shaped peptidoglycan cell wall, spore outgrowth
Gene expression levels in SubtiExpress: pbpA
Interactions involving this protein in SubtInteract: PbpA
MW, pI 79 kDa, 9.571
Gene length, protein length 2148 bp, 716 aa
Immediate neighbours pstS, yqgE
Sequences Protein DNA DNA_with_flanks
Genetic context
PbpA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PbpA expression.png















Categories containing this gene/protein

cell wall synthesis

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU25000

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jeff Errington lab
  • Antibody:

Labs working on this gene/protein

Jeff Errington, Newcastle University, UK homepage

Your additional remarks

References

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)

Ethan C Garner, Remi Bernard, Wenqin Wang, Xiaowei Zhuang, David Z Rudner, Tim Mitchison
Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis.
Science: 2011, 333(6039);222-5
[PubMed:21636745] [WorldCat.org] [DOI] (I p)

Julia Domínguez-Escobar, Arnaud Chastanet, Alvaro H Crevenna, Vincent Fromion, Roland Wedlich-Söldner, Rut Carballido-López
Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria.
Science: 2011, 333(6039);225-8
[PubMed:21636744] [WorldCat.org] [DOI] (I p)

Hanne-Leena Hyyryläinen, Bogumila C Marciniak, Kathleen Dahncke, Milla Pietiäinen, Pascal Courtin, Marika Vitikainen, Raili Seppala, Andreas Otto, Dörte Becher, Marie-Pierre Chapot-Chartier, Oscar P Kuipers, Vesa P Kontinen
Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis.
Mol Microbiol: 2010, 77(1);108-27
[PubMed:20487272] [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)

Yuping Wei, Teresa Havasy, Derrell C McPherson, David L Popham
Rod shape determination by the Bacillus subtilis class B penicillin-binding proteins encoded by pbpA and pbpH.
J Bacteriol: 2003, 185(16);4717-26
[PubMed:12896990] [WorldCat.org] [DOI] (P p)

T Murray, D L Popham, C B Pearson, A R Hand, P Setlow
Analysis of outgrowth of Bacillus subtilis spores lacking penicillin-binding protein 2a.
J Bacteriol: 1998, 180(24);6493-502
[PubMed:9851991] [WorldCat.org] [DOI] (P p)

T Murray, D L Popham, P Setlow
Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A.
J Bacteriol: 1997, 179(9);3021-9
[PubMed:9139922] [WorldCat.org] [DOI] (P p)