Difference between revisions of "RpsN"
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpsNA_141757_141942_1 rpsN] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpsNA_141757_141942_1 rpsN] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
** [[SigA]] two promoters, about 140bp and 200bp upstream of the start codon {{PubMed|9371452}} | ** [[SigA]] two promoters, about 140bp and 200bp upstream of the start codon {{PubMed|9371452}} | ||
| Line 141: | Line 141: | ||
=References= | =References= | ||
| − | + | <pubmed>17163968,8635744,9371452, 19648245 ,19653700 20208344 11948165 22517742 23002217</pubmed> | |
| − | <pubmed>17163968,8635744,9371452, 19648245 ,19653700 20208344 11948165 22517742</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 10:31, 19 June 2013
- Description: ribosomal protein
| Gene name | rpsN |
| Synonyms | |
| Essential | yes PubMed |
| Product | ribosomal protein S14 |
| Function | translation |
| Gene expression levels in SubtiExpress: rpsN | |
| Interactions involving this protein in SubtInteract: RpsN | |
| MW, pI | 7 kDa, 10.914 |
| Gene length, protein length | 183 bp, 61 aa |
| Immediate neighbours | rplE, rpsH |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
translation, essential genes, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01290
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ribosomal protein S14P family (according to Swiss-Prot) Zinc-binding S14P subfamily (according to Swiss-Prot)
- Paralogous protein(s): YhzA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- phosphorylated on Arg-41 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P12878
- KEGG entry: [2]
- E.C. number:
Additional information
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
- Regulatory mechanism:
- 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
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)
Hideaki Nanamiya, Fujio Kawamura
Towards an elucidation of the roles of the ribosome during different growth phases in Bacillus subtilis.
Biosci Biotechnol Biochem: 2010, 74(3);451-61
[PubMed:20208344]
[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)
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)
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)
