Difference between revisions of "RpsG"

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(Categories containing this gene/protein)
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* '''Modification:'''
 
* '''Modification:'''
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** phosphorylated on Arg-10 {{PubMed|22517742}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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=References=
 
=References=
<pubmed> 19653700 </pubmed>
+
<pubmed> 19653700 22517742</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:10, 21 April 2012

Gene name rpsG
Synonyms
Essential yes PubMed
Product ribosomal protein S7 (BS7)
Function translation
Interactions involving this protein in SubtInteract: RpsG
MW, pI 17 kDa, 10.456
Gene length, protein length 468 bp, 156 aa
Immediate neighbours rpsL, fusA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpsG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpsG expression.png
























Categories containing this gene/protein

translation, essential genes, universally conserved proteins, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01110

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-10 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1HUS (Geobacillus stearothermophilus)
  • 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)