RplK

• Description: ribosomal protein
  
  

Gene name	rplK
Synonyms	relC, tsp
Essential	no PubMed
Product	ribosomal protein L11 (BL11)
Function	translation
Gene expression levels in SubtiExpress: rplK
Interactions involving this protein in SubtInteract: RplK
MW, pI	14 kDa, 9.718
Gene length, protein length	423 bp, 141 aa
Immediate neighbours	nusG, rplA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, universally conserved proteins, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU01020

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein L11P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-94 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1FOX (C-terminal domain, Geobacillus stearothermophilus), 2FOW (RNA binding domain in complex with RNA, Geobacillus stearothermophilus)

• UniProt: Q06796

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: rplK PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

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)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Sascha Baumann, Sebastian Schoof, Marcel Bolten, Claudia Haering, Motoki Takagi, Kazuo Shin-ya, Hans-Dieter Arndt
Molecular determinants of microbial resistance to thiopeptide antibiotics.
J Am Chem Soc: 2010, 132(20);6973-81
[PubMed:20441189] [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)

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)

S Zhang, J M Scott, W G Haldenwang
Loss of ribosomal protein L11 blocks stress activation of the Bacillus subtilis transcription factor sigma(B).
J Bacteriol: 2001, 183(7);2316-21
[PubMed:11244072] [WorldCat.org] [DOI] (P p)

B Wienen, R Ehrlich, M Stöffler-Meilicke, G Stöffler, I Smith, D Weiss, R Vince, S Pestka
Ribosomal protein alterations in thiostrepton- and Micrococcin-resistant mutants of Bacillus subtilis.
J Biol Chem: 1979, 254(16);8031-41
[PubMed:112097] [WorldCat.org] (P p)