PbpA

• Description: penicillin-binding protein PBP 2A
  
  

Gene name	pbpA
Synonyms	yqgF
Essential	no
Product	penicillin-binding protein PBP 2A
Function	formation of a rod-shaped peptidoglycan cell wall, spore outgrowth
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
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 synthesis

The gene

Basic information

• Locus tag: BSU25000

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:
  • part of the cell wall biosynthetic complex PubMed
  • folding requires PrsA PubMed

• Localization: extracellular (signal peptide) PubMed

Database entries

• Structure:

• UniProt: P54488

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: pbpA PubMed

• Expression browser: pbpA PubMed

• Sigma factor:

• 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

References

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

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)