Difference between revisions of "RpmC"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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** [[Tig]]-[[RpmC]] {{PubMed|16271892,16091460}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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=References=
 
=References=
<pubmed>8635744,19653700 9371452 11948165 23002217</pubmed>
+
<pubmed>8635744,19653700 9371452 11948165 23002217 16271892,16091460</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:09, 20 August 2013

Gene name rpmC
Synonyms
Essential no PubMed
Product ribosomal protein L29
Function translation
Gene expression levels in SubtiExpress: rpmC
Interactions involving this protein in SubtInteract: RpmC
MW, pI 7 kDa, 10.628
Gene length, protein length 198 bp, 66 aa
Immediate neighbours rplP, rpsQ
Sequences Protein DNA DNA_with_flanks
Genetic context
RpmC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpmC expression.png















Categories containing this gene/protein

translation

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01240

Phenotypes of a mutant

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

  • 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

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)

Frank Schlünzen, Daniel N Wilson, Pingsheng Tian, Jörg M Harms, Stuart J McInnes, Harly A S Hansen, Renate Albrecht, Jörg Buerger, Sigurd M Wilbanks, Paola Fucini
The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction.
Structure: 2005, 13(11);1685-94
[PubMed:16271892] [WorldCat.org] [DOI] (P p)

David Baram, Erez Pyetan, Assa Sittner, Tamar Auerbach-Nevo, Anat Bashan, Ada Yonath
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action.
Proc Natl Acad Sci U S A: 2005, 102(34);12017-22
[PubMed:16091460] [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)