Difference between revisions of "RplM"
Line 32: | Line 32: | ||
<br/><br/> | <br/><br/> | ||
+ | |||
+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[translation]]}}, | ||
+ | {{SubtiWiki category|[[essential genes]]}} | ||
+ | |||
+ | = This gene is a member of the following [[regulons]] = | ||
+ | {{SubtiWiki regulon|[[stringent response]]}} | ||
=The gene= | =The gene= | ||
Line 53: | Line 60: | ||
− | + | ||
− | |||
− | |||
=The protein= | =The protein= | ||
Revision as of 15:41, 8 December 2010
- Description: ribosomal protein
Gene name | rplM |
Synonyms | |
Essential | yes PubMed |
Product | ribosomal protein L13 |
Function | translation |
MW, pI | 16 kDa, 10.176 |
Gene length, protein length | 435 bp, 145 aa |
Immediate neighbours | truA, rpsI |
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: BSU01490
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 L13P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- UniProt: P70974
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
Yuno Lee, Woo Young Bang, Songmi Kim, Prettina Lazar, Chul Wook Kim, Jeong Dong Bahk, Keun Woo Lee
Molecular modeling study for interaction between Bacillus subtilis Obg and Nucleotides.
PLoS One: 2010, 5(9);e12597
[PubMed:20830302]
[WorldCat.org]
[DOI]
(I e)
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)
Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165]
[WorldCat.org]
[DOI]
(P p)
J M Scott, J Ju, T Mitchell, W G Haldenwang
The Bacillus subtilis GTP binding protein obg and regulators of the sigma(B) stress response transcription factor cofractionate with ribosomes.
J Bacteriol: 2000, 182(10);2771-7
[PubMed:10781545]
[WorldCat.org]
[DOI]
(P p)