Difference between revisions of "RpsB"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[translation]]}}, | ||
| + | {{SubtiWiki category|[[essential genes]]}}, | ||
| + | {{SubtiWiki category|[[membrane proteins]]}}, | ||
| + | {{SubtiWiki category|[[universally conserved proteins]]}} | ||
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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 19:46, 8 December 2010
- Description: ribosomal protein
| Gene name | rpsB |
| Synonyms | |
| Essential | yes PubMed |
| Product | ribosomal protein S2 |
| Function | translation |
| MW, pI | 27 kDa, 6.256 |
| Gene length, protein length | 738 bp, 246 aa |
| Immediate neighbours | swrB, tsf |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
translation, essential genes, membrane proteins, universally conserved proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU16490
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ribosomal protein S2P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: membrane associated PubMed
Database entries
- Structure:
- UniProt: P21464
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
