PbpB

• Description: penicillin-binding protein 2B
  
  

Gene name	pbpB
Synonyms
Essential	yes PubMed
Product	penicillin-binding protein 2B
Function	septation
MW, pI	79 kDa, 9.234
Gene length, protein length	2148 bp, 716 aa
Immediate neighbours	ftsL, spoVD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell wall synthesis, essential genes, membrane proteins

The gene

Basic information

• Locus tag: BSU15160

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: transpeptidase family (according to Swiss-Prot)

• Paralogous protein(s): SpoVD

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • folding requires PrsA PubMed
  • PbpB-DivIB-(FtsL-DivIC)2 PubMed, as part of the divisome

• Localization: cell membrane PubMed, extracellular (signal peptide) PubMed, localizes to the sporulation septum during sporulation PubMed

Database entries

• Structure:

• UniProt: Q07868

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: mraZ-mraW-ftsL-pbpB PubMed

• Sigma factor:

• Regulation:
  • constitutively expressed PubMed

• Regulatory mechanism:

• Additional information:

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

Susan L Rowland, Kimberly D Wadsworth, Scott A Robson, Carine Robichon, Jon Beckwith, Glenn F King
Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.
J Bacteriol: 2010, 192(23);6116-25
[PubMed:20870765] [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)

Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628] [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)

Dirk-Jan Scheffers, Laura J F Jones, Jeffery Errington
Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis.
Mol Microbiol: 2004, 51(3);749-64
[PubMed:14731276] [WorldCat.org] [DOI] (P p)

R A Daniel, E J Harry, J Errington
Role of penicillin-binding protein PBP 2B in assembly and functioning of the division machinery of Bacillus subtilis.
Mol Microbiol: 2000, 35(2);299-311
[PubMed:10652091] [WorldCat.org] [DOI] (P p)

R A Daniel, A M Williams, J Errington
A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis.
J Bacteriol: 1996, 178(8);2343-50
[PubMed:8636036] [WorldCat.org] [DOI] (P p)

A Yanouri, R A Daniel, J Errington, C E Buchanan
Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis.
J Bacteriol: 1993, 175(23);7604-16
[PubMed:8244929] [WorldCat.org] [DOI] (P p)