RplW

• Description: ribosomal protein
  
  

Gene name	rplW
Synonyms
Essential	no PubMed
Product	ribosomal protein L23
Function	translation
Gene expression levels in SubtiExpress: rplW
Interactions involving this protein in SubtInteract: RplW
MW, pI	10 kDa, 10.087
Gene length, protein length	285 bp, 95 aa
Immediate neighbours	rplD, rplB
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, membrane proteins, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU01180

Database entries

• BsubCyc: BSU01180

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein L23P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-10 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • Tig-RplW PubMed
  • Map-RplW PubMed

• Localization:
  • membrane associated PubMed

Database entries

• BsubCyc: BSU01180

• Structure:

• UniProt: P42924

• 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: rplW 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:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Arzu Sandikci, Felix Gloge, Michael Martinez, Matthias P Mayer, Rebecca Wade, Bernd Bukau, Günter Kramer
Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.
Nat Struct Mol Biol: 2013, 20(7);843-50
[PubMed:23770820] [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)

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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I 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)

Günter Kramer, Thomas Rauch, Wolfgang Rist, Sonja Vorderwülbecke, Holger Patzelt, Agnes Schulze-Specking, Nenad Ban, Elke Deuerling, Bernd Bukau
L23 protein functions as a chaperone docking site on the ribosome.
Nature: 2002, 419(6903);171-4
[PubMed:12226666] [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)