RplB

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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
Get the DNA and protein sequences
(Barbe et al., 2009)
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)