Difference between revisions of "RpsF"
Line 79: | Line 79: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
+ | ** [[RpsF]]-[[RpsR]], the heterodimer binds the structure in the ''[[rpsF]]'' mRNA 5' UTR {{PubMed|24310371}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
Line 104: | Line 105: | ||
=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' ''[[yyaF]]-[[rpsF]]-[[ssbA]]-[[rpsR]]'' {{PubMed|14762004}} | + | * '''Operon:''' |
+ | ** ''[[yyaF]]-[[rpsF]]-[[ssbA]]-[[rpsR]]'' {{PubMed|14762004}} | ||
+ | ** ''[[rpsF]]-[[ssbA]]-[[rpsR]]'' {{PubMed|24310371,22383849}} | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpsF_4199445_4199732_-1 rpsF] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpsF_4199445_4199732_-1 rpsF] {{PubMed|22383849}} | ||
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
+ | ** ''[[rpsF]]'': [[SigA]] {{PubMed|24310371}} | ||
* '''Regulation:''' | * '''Regulation:''' | ||
Line 115: | Line 119: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** the mRNA contains a structured motif in the 5' UTR upstream of the ''[[rpsF]]'' ORF that is bound by [[RpsF]]-[[RpsR]] heterodimers and may be implicated in autogenous regulation {{PubMed|24310371}} | ||
=Biological materials = | =Biological materials = | ||
Line 135: | Line 140: | ||
=References= | =References= | ||
− | <pubmed>19653700 14762004 11948165 11948146 23002217</pubmed> | + | <pubmed>19653700 14762004 11948165 11948146 23002217 22383849 24310371 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:29, 13 December 2013
- Description: ribosomal protein
Gene name | rpsF |
Synonyms | |
Essential | no PubMed |
Product | ribosomal protein S6 (BS9) |
Function | translation |
Gene expression levels in SubtiExpress: rpsF | |
Interactions involving this protein in SubtInteract: RpsF | |
MW, pI | 10 kDa, 4.993 |
Gene length, protein length | 285 bp, 95 aa |
Immediate neighbours | ssbA, yyaF |
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
This gene is a member of the following regulons
ComK regulon, stringent response
The gene
Basic information
- Locus tag: BSU40910
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ribosomal protein S6P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure: 3R3T (from Bacillus anthracis, 71% identity, 97% similarity)
- UniProt: P21468
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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
Yang Fu, Kaila Deiorio-Haggar, Mark W Soo, Michelle M Meyer
Bacterial RNA motif in the 5' UTR of rpsF interacts with an S6:S18 complex.
RNA: 2014, 20(2);168-76
[PubMed:24310371]
[WorldCat.org]
[DOI]
(I p)
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)
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)
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)
Cordula Lindner, Reindert Nijland, Mariska van Hartskamp, Sierd Bron, Leendert W Hamoen, Oscar P Kuipers
Differential expression of two paralogous genes of Bacillus subtilis encoding single-stranded DNA binding protein.
J Bacteriol: 2004, 186(4);1097-105
[PubMed:14762004]
[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)
Mitsuo Ogura, Hirotake Yamaguchi, Kazuo Kobayashi, Naotake Ogasawara, Yasutaro Fujita, Teruo Tanaka
Whole-genome analysis of genes regulated by the Bacillus subtilis competence transcription factor ComK.
J Bacteriol: 2002, 184(9);2344-51
[PubMed:11948146]
[WorldCat.org]
[DOI]
(P p)