YtiA

• Description: general stress protein, binds in the stationary phase to the ribosome, replaces RpmE under conditions of zinc limitation
  
  

Gene name	ytiA
Synonyms	rpmE2, rpmEB
Essential	no
Product	accessory ribosomal protein
Function	survival of salt stress
Gene expression levels in SubtiExpress: ytiA
Interactions involving this protein in SubtInteract: YtiA
MW, pI	9 kDa, 9.808
Gene length, protein length	246 bp, 82 aa
Immediate neighbours	ytiB, ythA
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, general stress proteins (controlled by SigB), phosphoproteins

This gene is a member of the following regulons

SigB regulon, Zur regulon

The gene

Basic information

• Locus tag: BSU30700

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: Type B subfamily (according to Swiss-Prot)

• Paralogous protein(s): RpmE

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-70 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O34967

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: ytiA PubMed

• Expression browser: ytiA PubMed

• Sigma factor: SigB PubMed

• Regulation:
  • induced by stress (SigB) PubMed
  • induced by zinc starvation (Zur) PubMed

• Regulatory mechanism:
  • Zur: transcription repression in the presence of zinc PubMed

• Additional information:

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)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Scott E Gabriel, John D Helmann
Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions.
J Bacteriol: 2009, 191(19);6116-22
[PubMed:19648245] [WorldCat.org] [DOI] (I p)

Yousuke Natori, Hideaki Nanamiya, Genki Akanuma, Saori Kosono, Toshiaki Kudo, Kozo Ochi, Fujio Kawamura
A fail-safe system for the ribosome under zinc-limiting conditions in Bacillus subtilis.
Mol Microbiol: 2007, 63(1);294-307
[PubMed:17163968] [WorldCat.org] [DOI] (P p)

Genki Akanuma, Hideaki Nanamiya, Yousuke Natori, Naofumi Nomura, Fujio Kawamura
Liberation of zinc-containing L31 (RpmE) from ribosomes by its paralogous gene product, YtiA, in Bacillus subtilis.
J Bacteriol: 2006, 188(7);2715-20
[PubMed:16547061] [WorldCat.org] [DOI] (P p)

Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528] [WorldCat.org] [DOI] (P p)

Hideaki Nanamiya, Genki Akanuma, Yousuke Natori, Rikinori Murayama, Saori Kosono, Toshiaki Kudo, Kazuo Kobayashi, Naotake Ogasawara, Seung-Moon Park, Kozo Ochi, Fujio Kawamura
Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome.
Mol Microbiol: 2004, 52(1);273-83
[PubMed:15049826] [WorldCat.org] [DOI] (P p)

Ekaterina M Panina, Andrey A Mironov, Mikhail S Gelfand
Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins.
Proc Natl Acad Sci U S A: 2003, 100(17);9912-7
[PubMed:12904577] [WorldCat.org] [DOI] (P p)