Difference between revisions of "PbpB"
Line 76: | Line 76: | ||
* '''Interactions:''' | * '''Interactions:''' | ||
** folding requires [[PrsA]] {{PubMed|20487272}} | ** folding requires [[PrsA]] {{PubMed|20487272}} | ||
+ | ** [[PbpB]]-[[DivIB]]-([[FtsL]]-[[DivIC]])2 {{PubMed|20870765}}, as part of the [[divisome]] | ||
* '''Localization:''' cell membrane (according to Swiss-Prot), extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed], localizes to the sporulation septum during sporulation [http://www.ncbi.nlm.nih.gov/sites/entrez/15758244 PubMed] | * '''Localization:''' cell membrane (according to Swiss-Prot), extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed], localizes to the sporulation septum during sporulation [http://www.ncbi.nlm.nih.gov/sites/entrez/15758244 PubMed] | ||
Line 126: | Line 127: | ||
=References= | =References= | ||
− | <pubmed>8636036,14731276,8244929,20487272,10652091, 19429628, 18957862 </pubmed> | + | <pubmed>8636036,14731276,8244929,20487272,10652091, 19429628, 18957862 20870765 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:38, 28 September 2010
- 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
|
Contents
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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot), extracellular (signal peptide) PubMed, localizes to the sporulation septum during sporulation PubMed
Database entries
- Structure:
- 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
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)