Difference between revisions of "RplB"

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Revision as of 12:22, 16 May 2013

Gene name rplB
Synonyms
Essential yes PubMed
Product ribosomal protein L2 (BL2)
Function translation
Gene expression levels in SubtiExpress: rplB
Interactions involving this protein in SubtInteract: RplB
MW, pI 30 kDa, 11.013
Gene length, protein length 831 bp, 277 aa
Immediate neighbours rplW, rpsS
Sequences Protein DNA DNA_with_flanks
Genetic context
RplB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplB expression.png















Categories containing this gene/protein

translation, essential genes, universally conserved proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01190

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: 1RL2 (L2 RNA-binding domain, 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

Additional publications: PubMed

Josephine R Chandler, Thao T Truong, Patricia M Silva, Mohammad R Seyedsayamdost, Gavin Carr, Matthew Radey, Michael A Jacobs, Elizabeth H Sims, Jon Clardy, E Peter Greenberg
Bactobolin resistance is conferred by mutations in the L2 ribosomal protein.
mBio: 2012, 3(6);
[PubMed:23249812] [WorldCat.org] [DOI] (I e)

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)

A Nakagawa, T Nakashima, M Taniguchi, H Hosaka, M Kimura, I Tanaka
The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome.
EMBO J: 1999, 18(6);1459-67
[PubMed:10075918] [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)