Difference between revisions of "RplM"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU01490&redirect=T BSU01490] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
| Line 97: | Line 98: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU01490&redirect=T BSU01490] | ||
* '''Structure:''' | * '''Structure:''' | ||
Revision as of 12:50, 2 April 2014
- Description: ribosomal protein
| Gene name | rplM |
| Synonyms | |
| Essential | yes PubMed |
| Product | ribosomal protein L13 |
| Function | translation |
| Gene expression levels in SubtiExpress: rplM | |
| Interactions involving this protein in SubtInteract: RplM | |
| MW, pI | 16 kDa, 10.176 |
| Gene length, protein length | 435 bp, 145 aa |
| Immediate neighbours | truA, rpsI |
| 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: BSU01490
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU01490
- 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:
Database entries
- BsubCyc: BSU01490
- Structure:
- UniProt: P70974
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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)
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)
