Difference between revisions of "PcrB"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | {{SubtiWiki category|[[ | + | {{SubtiWiki category|[[lipid metabolism/ other]]}} |
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
Revision as of 09:15, 23 May 2012
- Description: heptaprenylglyceryl phosphate synthase
| Gene name | pcrB |
| Synonyms | yerE |
| Essential | no |
| Product | heptaprenylglyceryl phosphate synthase |
| Function | unknown |
| MW, pI | 24 kDa, 4.204 |
| Gene length, protein length | 684 bp, 228 aa |
| Immediate neighbours | yerD, pcrA |
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU06600
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: GGGP synthase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1VIZ
- UniProt: O34790
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
David Peterhoff, Hermann Zellner, Harald Guldan, Rainer Merkl, Reinhard Sterner, Patrick Babinger
Dimerization determines substrate specificity of a bacterial prenyltransferase.
Chembiochem: 2012, 13(9);1297-303
[PubMed:22614947]
[WorldCat.org]
[DOI]
(I p)
Harald Guldan, Frank-Michael Matysik, Marco Bocola, Reinhard Sterner, Patrick Babinger
Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria.
Angew Chem Int Ed Engl: 2011, 50(35);8188-91
[PubMed:21761520]
[WorldCat.org]
[DOI]
(I p)
Harald Guldan, Reinhard Sterner, Patrick Babinger
Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.
Biochemistry: 2008, 47(28);7376-84
[PubMed:18558723]
[WorldCat.org]
[DOI]
(I p)
M A Petit, E Dervyn, M Rose, K D Entian, S McGovern, S D Ehrlich, C Bruand
PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication.
Mol Microbiol: 1998, 29(1);261-73
[PubMed:9701819]
[WorldCat.org]
[DOI]
(P p)
