Difference between revisions of "RpmB"

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(References)
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=References=
 
=References=
'''Additional publications:''' {{PubMed|23002217,23033921}}
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<pubmed>19653700 23002217,23033921</pubmed>
<pubmed>19653700 </pubmed>
 
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:58, 4 June 2013

Gene name rpmB
Synonyms yloT
Essential no PubMed
Product ribosomal protein L28
Function translation
Gene expression levels in SubtiExpress: rpmB
Interactions involving this protein in SubtInteract: RpmB
MW, pI 6 kDa, 12.242
Gene length, protein length 186 bp, 62 aa
Immediate neighbours spoVM, yloU
Sequences Protein DNA DNA_with_flanks
Genetic context
RpmB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpmB expression.png















Categories containing this gene/protein

translation

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU15820

Phenotypes of a mutant

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:
  • Sigma factor:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • strongly repressed in response to glucose starvation in M9 medium 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

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

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)

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)