Difference between revisions of "RplW"
| Line 92: | Line 92: | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
| + | ** [[Tig]]-[[RplW]] {{PubMed|16271892,16091460}} | ||
| − | * '''[[Localization]]:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | + | * '''[[Localization]]:''' |
| + | ** membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
=== Database entries === | === Database entries === | ||
| Line 141: | Line 143: | ||
=References= | =References= | ||
| − | <pubmed>18763711, 19653700 9371452 11948165 8635744 22517742 23002217</pubmed> | + | <pubmed>18763711, 19653700 9371452 11948165 8635744 22517742 23002217 16271892,16091460</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:09, 20 August 2013
- Description: ribosomal protein
| Gene name | rplW |
| Synonyms | |
| Essential | no PubMed |
| Product | ribosomal protein L23 |
| Function | translation |
| Gene expression levels in SubtiExpress: rplW | |
| Interactions involving this protein in SubtInteract: RplW | |
| MW, pI | 10 kDa, 10.087 |
| Gene length, protein length | 285 bp, 95 aa |
| Immediate neighbours | rplD, rplB |
| 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, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01180
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: ribosomal protein L23P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- phosphorylated on Arg-10 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- membrane associated PubMed
Database entries
- Structure:
- UniProt: P42924
- 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)
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)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Frank Schlünzen, Daniel N Wilson, Pingsheng Tian, Jörg M Harms, Stuart J McInnes, Harly A S Hansen, Renate Albrecht, Jörg Buerger, Sigurd M Wilbanks, Paola Fucini
The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction.
Structure: 2005, 13(11);1685-94
[PubMed:16271892]
[WorldCat.org]
[DOI]
(P p)
David Baram, Erez Pyetan, Assa Sittner, Tamar Auerbach-Nevo, Anat Bashan, Ada Yonath
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action.
Proc Natl Acad Sci U S A: 2005, 102(34);12017-22
[PubMed:16091460]
[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)
