RplV

• Description: ribosomal protein
  
  

Gene name	rplV
Synonyms
Essential	no PubMed
Product	ribosomal protein L22 (BL17)
Function	translation
Gene expression levels in SubtiExpress: rplV
Interactions involving this protein in SubtInteract: RplV
MW, pI	12 kDa, 11.225
Gene length, protein length	339 bp, 113 aa
Immediate neighbours	rpsS, rpsC
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, universally conserved proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU01210

Database entries

• BsubCyc: BSU01210

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein L22P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • DefA-RplV PubMed

• Localization:

Database entries

• BsubCyc: BSU01210

• Structure:

• UniProt: P42060

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: rpsJ-rplC-rplD-rplW-rplB-rpsS-rplV-rpsC-rplP-rpmC-rpsQ-rplN-rplX-rplE-rpsN-rpsH-rplF-rplR-rpsE-rpmD-rplO PubMed

• Expression browser: rplV PubMed

• 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:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 3908 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 4954 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Rouven Bingel-Erlenmeyer, Rebecca Kohler, Günter Kramer, Arzu Sandikci, Snjezana Antolić, Timm Maier, Christiane Schaffitzel, Brigitte Wiedmann, Bernd Bukau, Nenad Ban
A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing.
Nature: 2008, 452(7183);108-11
[PubMed:18288106] [WorldCat.org] [DOI] (I 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)