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

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
RplM context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplM expression.png















Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

stringent response

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:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • 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)