Difference between revisions of "PbpB"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15160&redirect=T BSU15160] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yllB-ylxA-ftsL-pbpB.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yllB-ylxA-ftsL-pbpB.html] | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15160&redirect=T BSU15160] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1rp5 1RP5] (PBP 2x from ''Streptococcus pneumoniae'', 32% identity) {{PubMed|14734544}} | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1rp5 1RP5] (PBP 2x from ''Streptococcus pneumoniae'', 32% identity) {{PubMed|14734544}} |
Revision as of 13:38, 2 April 2014
- Description: class B penicillin-binding protein 2B, Pbp2B
Gene name | pbpB |
Synonyms | |
Essential | yes PubMed |
Product | penicillin-binding protein 2B |
Function | septation, cell division |
Gene expression levels in SubtiExpress: pbpB | |
Interactions involving this protein in SubtInteract: PbpB | |
MW, pI | 79 kDa, 9.234 |
Gene length, protein length | 2148 bp, 716 aa |
Immediate neighbours | ftsL, spoVD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell wall synthesis, cell division, essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15160
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU15160
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU15160
- UniProt: Q07868
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Your additional remarks
References
Katharina Peters, Inga Schweizer, Katrin Beilharz, Christoph Stahlmann, Jan-Willem Veening, Regine Hakenbeck, Dalia Denapaite
Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance.
Mol Microbiol: 2014, 92(4);733-55
[PubMed:24655324]
[WorldCat.org]
[DOI]
(I p)
Marta Carolina Afonso Lages, Katrin Beilharz, Danae Morales Angeles, Jan-Willem Veening, Dirk-Jan Scheffers
The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability.
Environ Microbiol: 2013, 15(12);3272-81
[PubMed:23895585]
[WorldCat.org]
[DOI]
(I p)
Tatsuya Fukushima, Isako Furihata, Robyn Emmins, Richard A Daniel, James A Hoch, Hendrik Szurmant
A role for the essential YycG sensor histidine kinase in sensing cell division.
Mol Microbiol: 2011, 79(2);503-22
[PubMed:21219466]
[WorldCat.org]
[DOI]
(I p)
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)
Lucile Pernot, Laurent Chesnel, Audrey Le Gouellec, Jacques Croizé, Thierry Vernet, Otto Dideberg, Andréa Dessen
A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics.
J Biol Chem: 2004, 279(16);16463-70
[PubMed:14734544]
[WorldCat.org]
[DOI]
(P 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)