Difference between revisions of "RplQ"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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** [[Map]]-[[RplQ]] {{PubMed|23770820}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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=References=
 
=References=
<pubmed>8635744,23002217, 19653700 </pubmed>
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<pubmed>8635744,23002217, 19653700 23770820</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:28, 20 August 2013

Gene name rplQ
Synonyms
Essential yes PubMed
Product ribosomal protein L17 (BL15)
Function translation
Gene expression levels in SubtiExpress: rplQ
Interactions involving this protein in SubtInteract: RplQ
MW, pI 13 kDa, 10.265
Gene length, protein length 360 bp, 120 aa
Immediate neighbours rpoA, ybxA
Sequences Protein DNA DNA_with_flanks
Genetic context
RplQ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplQ 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: BSU01440

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

Arzu Sandikci, Felix Gloge, Michael Martinez, Matthias P Mayer, Rebecca Wade, Bernd Bukau, Günter Kramer
Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.
Nat Struct Mol Biol: 2013, 20(7);843-50
[PubMed:23770820] [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)

J W Suh, S A Boylan, S H Oh, C W Price
Genetic and transcriptional organization of the Bacillus subtilis spc-alpha region.
Gene: 1996, 169(1);17-23
[PubMed:8635744] [WorldCat.org] [DOI] (P p)