Difference between revisions of "PbpB"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1rp5 1RP5] (PBP 2x from [[Streptococcus pneumoniae]], 32% identity) {{PubMed|14734544}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/Q07868 Q07868] | * '''UniProt:''' [http://www.uniprot.org/uniprot/Q07868 Q07868] | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pbpB_1581947_1584097_1 pbpB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pbpB_1581947_1584097_1 pbpB] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
| − | <pubmed>8636036,14731276,8244929,20487272,10652091, 19429628, 18957862 21219466 20870765</pubmed> | + | <pubmed>8636036,14731276,8244929,20487272,10652091, 19429628, 18957862 21219466 20870765 14734544 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 15:47, 29 January 2014
- Description: penicillin-binding protein 2B, Pbp2B
| Gene name | pbpB |
| Synonyms | |
| Essential | yes PubMed |
| Product | penicillin-binding protein 2B |
| Function | septation |
| 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, 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
- 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
- Structure: 1RP5 (PBP 2x from Streptococcus pneumoniae, 32% identity) PubMed
- 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
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)
