Difference between revisions of "PbpB"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || septation | |style="background:#ABCDEF;" align="center"|'''Function''' || septation | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU15160 pbpB] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/PbpB PbpB] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/PbpB PbpB] | ||
| Line 24: | Line 24: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ftsL]]'', ''[[spoVD]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ftsL]]'', ''[[spoVD]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15160 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15160 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15160 Advanced_DNA] |
|- | |- | ||
|- | |- | ||
Revision as of 12:45, 13 May 2013
- Description: penicillin-binding protein 2B
| 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 Advanced_DNA |
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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: Q07868
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Your additional remarks
References
Additional references: PubMed
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)
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)
Rut Carballido-López, Alex Formstone, Ying Li, S Dusko Ehrlich, Philippe Noirot, Jeff Errington
Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.
Dev Cell: 2006, 11(3);399-409
[PubMed:16950129]
[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)
