Difference between revisions of "RplN"

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(Categories containing this gene/protein)
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* '''Modification:'''
 
* '''Modification:'''
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** phosphorylated on Arg-7 {{PubMed|22517742}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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=References=
 
=References=
  
<pubmed>8635744,19653700 9371452 11948165</pubmed>
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<pubmed>8635744,19653700 9371452 11948165 22517742</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:10, 21 April 2012

Gene name rplN
Synonyms
Essential yes PubMed
Product ribosomal protein L14
Function translation
Interactions involving this protein in SubtInteract: RplN
MW, pI 13 kDa, 10.399
Gene length, protein length 366 bp, 122 aa
Immediate neighbours rpsQ, rplX
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RplN context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplN 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: BSU01260

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-7 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1WHI (Geobacillus stearothermophilus)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
    • SigA two promoters, about 140bp and 200bp upstream of the start codon PubMed
  • 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)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

X Li, L Lindahl, Y Sha, J M Zengel
Analysis of the Bacillus subtilis S10 ribosomal protein gene cluster identifies two promoters that may be responsible for transcription of the entire 15-kilobase S10-spc-alpha cluster.
J Bacteriol: 1997, 179(22);7046-54
[PubMed:9371452] [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)