Difference between revisions of "RpsL"

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(Categories containing this gene/protein)
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* '''Modification:'''
 
* '''Modification:'''
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** phosphorylated on Arg-123 {{PubMed|22517742}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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=References=
 
=References=
<pubmed> 19653700 11489846 16391027 </pubmed>
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<pubmed> 19653700 11489846 16391027 22517742</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:11, 21 April 2012

Gene name rpsL
Synonyms strA, fun
Essential yes PubMed
Product ribosomal protein S12 (BS12)
Function translation
Interactions involving this protein in SubtInteract: RpsL
MW, pI 15 kDa, 11.721
Gene length, protein length 414 bp, 138 aa
Immediate neighbours ybxF, rpsG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpsL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpsL expression.png
























Categories containing this gene/protein

translation, essential genes, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01100

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:
    • phosphorylated on Arg-123 PubMed
  • 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
  • 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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [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)

Kazuhiko Kurosawa, Takeshi Hosaka, Norimasa Tamehiro, Takashi Inaoka, Kozo Ochi
Improvement of alpha-amylase production by modulation of ribosomal component protein S12 in Bacillus subtilis 168.
Appl Environ Microbiol: 2006, 72(1);71-7
[PubMed:16391027] [WorldCat.org] [DOI] (P p)

T Inaoka, K Kasai, K Ochi
Construction of an in vivo nonsense readthrough assay system and functional analysis of ribosomal proteins S12, S4, and S5 in Bacillus subtilis.
J Bacteriol: 2001, 183(17);4958-63
[PubMed:11489846] [WorldCat.org] [DOI] (P p)