Difference between revisions of "RpmE"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[translation]]}}, | ||
| + | {{SubtiWiki category|[[essential genes]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[stringent response]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 00:20, 9 December 2010
- Description: ribosomal protein
| Gene name | rpmE |
| Synonyms | |
| Essential | yes PubMed |
| Product | ribosomal protein L31 |
| Function | translation |
| MW, pI | 7 kDa, 9.157 |
| Gene length, protein length | 198 bp, 66 aa |
| Immediate neighbours | tdk, rho |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU37070
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: Type A subfamily (according to Swiss-Prot)
- Paralogous protein(s): YtiA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: Zn(2+) PubMed
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: Q03223
- KEGG entry: [3]
- E.C. number:
Additional information
Under conditions of zinc starvation, RpmE is replaced by its paralog YtiA, that does not require zinc PubMed
Expression and regulation
- Operon: rpmE PubMed
- Sigma factor:
- 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
Hideaki Nanamiya, Fujio Kawamura
Towards an elucidation of the roles of the ribosome during different growth phases in Bacillus subtilis.
Biosci Biotechnol Biochem: 2010, 74(3);451-61
[PubMed:20208344]
[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)
Yousuke Natori, Hideaki Nanamiya, Genki Akanuma, Saori Kosono, Toshiaki Kudo, Kozo Ochi, Fujio Kawamura
A fail-safe system for the ribosome under zinc-limiting conditions in Bacillus subtilis.
Mol Microbiol: 2007, 63(1);294-307
[PubMed:17163968]
[WorldCat.org]
[DOI]
(P p)
Hideaki Nanamiya, Genki Akanuma, Yousuke Natori, Rikinori Murayama, Saori Kosono, Toshiaki Kudo, Kazuo Kobayashi, Naotake Ogasawara, Seung-Moon Park, Kozo Ochi, Fujio Kawamura
Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome.
Mol Microbiol: 2004, 52(1);273-83
[PubMed:15049826]
[WorldCat.org]
[DOI]
(P p)
