Difference between revisions of "YtiA"
Line 102: | Line 102: | ||
* '''Operon:''' | * '''Operon:''' | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpmEB_3138978_3139226_-1 ytiA] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] | ||
* '''Regulation:''' induced by stress ([[SigB]]) [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] | * '''Regulation:''' induced by stress ([[SigB]]) [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] | ||
Line 110: | Line 112: | ||
** [[Zur]]: transcription repression in the presence of zinc [http://www.ncbi.nlm.nih.gov/sites/entrez/12904577,15049826 PubMed] | ** [[Zur]]: transcription repression in the presence of zinc [http://www.ncbi.nlm.nih.gov/sites/entrez/12904577,15049826 PubMed] | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = |
Revision as of 15:55, 16 April 2012
- Description: general stress protein, binds in the stationary phase to the ribosome, replaces RpmE under conditions of zinc limitation
Gene name | ytiA |
Synonyms | |
Essential | no |
Product | accessory ribosomal protein |
Function | survival of salt stress |
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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
translation, general stress proteins (controlled by SigB)
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU30700
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
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:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O34967
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)