Difference between revisions of "MenB"
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 929 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 2531 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = |
Revision as of 09:41, 17 April 2014
- Description: naphthoate synthase
Gene name | menB |
Synonyms | |
Essential | yes PubMed |
Product | naphthoate synthase |
Function | biosynthesis of menaquinone |
Gene expression levels in SubtiExpress: menB | |
Metabolic function and regulation of this protein in SubtiPathways: menB | |
MW, pI | 29 kDa, 5.343 |
Gene length, protein length | 813 bp, 271 aa |
Immediate neighbours | menE, ytxM |
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
biosynthesis of cofactors, essential genes, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU30800
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU30800
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: o-succinylbenzoyl-CoA = CoA + 1,4-dihydroxy-2-naphthoate (according to Swiss-Prot)
- Protein family: enoyl-CoA hydratase/isomerase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- phosphorylated on Arg-78 and Arg-269 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU30800
- Structure: 1RJM (from Mycobacterium tuberculosis, 48% identity, 61% similarity)
- UniProt: P23966
- KEGG entry: [3]
- E.C. number: 4.1.3.36
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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221]
[WorldCat.org]
[DOI]
(P p)
X Qin, H W Taber
Transcriptional regulation of the Bacillus subtilis menp1 promoter.
J Bacteriol: 1996, 178(3);705-13
[PubMed:8550504]
[WorldCat.org]
[DOI]
(P p)
J R Driscoll, H W Taber
Sequence organization and regulation of the Bacillus subtilis menBE operon.
J Bacteriol: 1992, 174(15);5063-71
[PubMed:1629163]
[WorldCat.org]
[DOI]
(P p)