Difference between revisions of "PbpD"
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|style="background:#ABCDEF;" align="center"|'''Function''' || bifunctional glucosyltransferase/ transpeptidase | |style="background:#ABCDEF;" align="center"|'''Function''' || bifunctional glucosyltransferase/ transpeptidase | ||
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| + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU31490 pbpD] | ||
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|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/PbpD PbpD] | |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/PbpD PbpD] | ||
Revision as of 15:26, 7 August 2012
- Description: penicillin-binding protein 4
| Gene name | pbpD |
| Synonyms | |
| Essential | no |
| Product | penicillin-binding protein 4 |
| Function | bifunctional glucosyltransferase/ transpeptidase |
| Gene expression levels in SubtiExpress: pbpD | |
| Interactions involving this protein in SubtInteract: PbpD | |
| MW, pI | 70 kDa, 9.307 |
| Gene length, protein length | 1872 bp, 624 aa |
| Immediate neighbours | yuxJ, yuxK |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
cell wall synthesis, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31490
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P40750
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)
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)
D L Popham, P Setlow
Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular-weight penicillin-binding proteins.
J Bacteriol: 1996, 178(7);2079-85
[PubMed:8606187]
[WorldCat.org]
[DOI]
(P p)
D L Popham, P Setlow
Cloning, nucleotide sequence, mutagenesis, and mapping of the Bacillus subtilis pbpD gene, which codes for penicillin-binding protein 4.
J Bacteriol: 1994, 176(23);7197-205
[PubMed:7961491]
[WorldCat.org]
[DOI]
(P p)
