Difference between revisions of "RplL"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** [[YsxC]]-[[RplL]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17981968 PubMed]
 
** [[YsxC]]-[[RplL]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17981968 PubMed]
 +
** [[FusA]]-[[RplL]] {{PubMed|23912278}}
  
 
* '''[[Localization]]:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
 
* '''[[Localization]]:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
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=References=
 
=References=
<pubmed>7657605,17981968,,18763711, 19653700 23002217</pubmed>
+
<pubmed>7657605,17981968,23912278,18763711, 19653700 23002217</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:30, 20 August 2013

Gene name rplL
Synonyms
Essential yes PubMed
Product ribosomal protein L12 (BL9)
Function translation
Gene expression levels in SubtiExpress: rplL
Interactions involving this protein in SubtInteract: RplL
MW, pI 12 kDa, 4.355
Gene length, protein length 369 bp, 123 aa
Immediate neighbours rplJ, ybxB
Sequences Protein DNA DNA_with_flanks
Genetic context
RplL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplL expression.png















Categories containing this gene/protein

translation, essential genes, membrane proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01050

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

Yun Chen, Shu Feng, Veerendra Kumar, Rya Ero, Yong-Gui Gao
Structure of EF-G-ribosome complex in a pretranslocation state.
Nat Struct Mol Biol: 2013, 20(9);1077-84
[PubMed:23912278] [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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Catherine Wicker-Planquart, Anne-Emmanuelle Foucher, Mathilde Louwagie, Robert A Britton, Jean-Michel Jault
Interactions of an essential Bacillus subtilis GTPase, YsxC, with ribosomes.
J Bacteriol: 2008, 190(2);681-90
[PubMed:17981968] [WorldCat.org] [DOI] (I p)

K J Boor, M L Duncan, C W Price
Genetic and transcriptional organization of the region encoding the beta subunit of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(35);20329-36
[PubMed:7657605] [WorldCat.org] [DOI] (P p)