RpsL

• Description: ribosomal protein
  
  

Gene name	rpsL
Synonyms	strA, fun
Essential	yes PubMed
Product	ribosomal protein S12 (BS12)
Function	translation
Gene expression levels in SubtiExpress: rpsL
Interactions involving this protein in SubtInteract: RpsL
MW, pI	15 kDa, 11.721
Gene length, protein length	414 bp, 138 aa
Immediate neighbours	ybxF, rpsG
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, essential genes, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU01100

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein S12P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-123 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P21472

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: rpsL PubMed

• Sigma factor:

• 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

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)

Kazuhiko Kurosawa, Takeshi Hosaka, Norimasa Tamehiro, Takashi Inaoka, Kozo Ochi
Improvement of alpha-amylase production by modulation of ribosomal component protein S12 in Bacillus subtilis 168.
Appl Environ Microbiol: 2006, 72(1);71-7
[PubMed:16391027] [WorldCat.org] [DOI] (P p)

T Inaoka, K Kasai, K Ochi
Construction of an in vivo nonsense readthrough assay system and functional analysis of ribosomal proteins S12, S4, and S5 in Bacillus subtilis.
J Bacteriol: 2001, 183(17);4958-63
[PubMed:11489846] [WorldCat.org] [DOI] (P p)