Difference between revisions of "RpmD"

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|colspan="2" | '''Genetic context''' <br/> [[Image:rpmD_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:rpmD_context.gif]]
 
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpmD_143875_144054_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:rpmD_expression.png|500px]]
 
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Revision as of 12:58, 18 April 2012

Gene name rpmD
Synonyms
Essential yes PubMed
Product ribosomal protein L30 (BL27)
Function translation
Interactions involving this protein in SubtInteract: RpmD
MW, pI 6 kDa, 10.799
Gene length, protein length 177 bp, 59 aa
Immediate neighbours rpsE, rplO
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpmD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpmD 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: BSU01340

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

  • 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

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)