Difference between revisions of "RpmGA"

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(Basic information/ Evolution)
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* '''Protein family:''' [[ribosomal protein]] L33P family (according to Swiss-Prot)
 
* '''Protein family:''' [[ribosomal protein]] L33P family (according to Swiss-Prot)
  
* '''Paralogous protein(s):''' [[RpmGB]], [[RpmGC/1|RpmGC]]
+
* '''Paralogous protein(s):''' [[RpmGB]], [[RpmGC]]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===

Revision as of 15:59, 6 February 2015

Gene name rpmGA
Synonyms
Essential no PubMed
Product ribosomal protein L33a
Function translation
Gene expression levels in SubtiExpress: rpmGA
Interactions involving this protein in SubtInteract: RpmGA
MW, pI 5 kDa, 10.436
Gene length, protein length 147 bp, 49 aa
Immediate neighbours yqgN, yqgM
Sequences Protein DNA DNA_with_flanks
Genetic context
RpmGA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpmGA expression.png















Categories containing this gene/protein

translation, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU24900

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylated on Arg-29 PubMed
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

  • the protein is significantly underrepresented in 45S assembly intermediates that accumulate upon depletion of RbgA PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • 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

Ahmad Jomaa, Nikhil Jain, Joseph H Davis, James R Williamson, Robert A Britton, Joaquin Ortega
Functional domains of the 50S subunit mature late in the assembly process.
Nucleic Acids Res: 2014, 42(5);3419-35
[PubMed:24335279] [WorldCat.org] [DOI] (I p)

Ningning Li, Yuling Chen, Qiang Guo, Yixiao Zhang, Yi Yuan, Chengying Ma, Haiteng Deng, Jianlin Lei, Ning Gao
Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.
Nucleic Acids Res: 2013, 41(14);7073-83
[PubMed:23700310] [WorldCat.org] [DOI] (I p)

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)

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)

Scott E Gabriel, John D Helmann
Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions.
J Bacteriol: 2009, 191(19);6116-22
[PubMed:19648245] [WorldCat.org] [DOI] (I p)