Difference between revisions of "RpmGB"
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpmGB_117349_117498_1 rpmGB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpmGB_117349_117498_1 rpmGB] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
| Line 135: | Line 135: | ||
=References= | =References= | ||
| − | + | <pubmed> 19648245 19653700 23002217</pubmed> | |
| − | <pubmed> 19648245 19653700 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 10:22, 19 June 2013
- Description: ribosomal protein
| Gene name | rpmGB |
| Synonyms | rpmG |
| Essential | no PubMed |
| Product | ribosomal protein L33b |
| Function | translation |
| Gene expression levels in SubtiExpress: rpmGB | |
| Interactions involving this protein in SubtInteract: RpmGB | |
| MW, pI | 5 kDa, 9.893 |
| Gene length, protein length | 147 bp, 49 aa |
| Immediate neighbours | sigH, secE |
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00990
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ribosomal protein L33P family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: Q06798
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
Genki Akanuma, Hideaki Nanamiya, Yousuke Natori, Koichi Yano, Shota Suzuki, Shuya Omata, Morio Ishizuka, Yasuhiko Sekine, Fujio Kawamura
Inactivation of ribosomal protein genes in Bacillus subtilis reveals importance of each ribosomal protein for cell proliferation and cell differentiation.
J Bacteriol: 2012, 194(22);6282-91
[PubMed:23002217]
[WorldCat.org]
[DOI]
(I p)
Matthew A Lauber, William E Running, James P Reilly
B. subtilis ribosomal proteins: structural homology and post-translational modifications.
J Proteome Res: 2009, 8(9);4193-206
[PubMed:19653700]
[WorldCat.org]
[DOI]
(P p)
Scott E Gabriel, John D Helmann
Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions.
J Bacteriol: 2009, 191(19);6116-22
[PubMed:19648245]
[WorldCat.org]
[DOI]
(I p)
