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
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 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

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)