Difference between revisions of "RplL"
| Line 42: | Line 42: | ||
{{SubtiWiki category|[[translation]]}}, | {{SubtiWiki category|[[translation]]}}, | ||
{{SubtiWiki category|[[essential genes]]}}, | {{SubtiWiki category|[[essential genes]]}}, | ||
| − | {{SubtiWiki category|[[membrane proteins]]}} | + | {{SubtiWiki category|[[membrane proteins]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| Line 64: | Line 65: | ||
=== Additional information=== | === Additional information=== | ||
| − | |||
| − | |||
| − | |||
=The protein= | =The protein= | ||
| Line 82: | Line 80: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| Line 122: | Line 120: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
| Line 142: | Line 141: | ||
=References= | =References= | ||
| − | <pubmed>7657605,17981968,23912278,18763711, 19653700 23002217</pubmed> | + | <pubmed>7657605,17981968,23912278,18763711, 19653700 23002217 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:54, 5 March 2014
- Description: ribosomal protein
| Gene name | rplL |
| Synonyms | |
| Essential | yes PubMed |
| Product | ribosomal protein L12 (BL9) |
| Function | translation |
| Gene expression levels in SubtiExpress: rplL | |
| Interactions involving this protein in SubtInteract: RplL | |
| MW, pI | 12 kDa, 4.355 |
| Gene length, protein length | 369 bp, 123 aa |
| Immediate neighbours | rplJ, ybxB |
| 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, membrane proteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01050
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 L12P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: membrane associated PubMed
Database entries
- Structure:
- UniProt: P02394
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulatory mechanism:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Yun Chen, Shu Feng, Veerendra Kumar, Rya Ero, Yong-Gui Gao
Structure of EF-G-ribosome complex in a pretranslocation state.
Nat Struct Mol Biol: 2013, 20(9);1077-84
[PubMed:23912278]
[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)
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)
Catherine Wicker-Planquart, Anne-Emmanuelle Foucher, Mathilde Louwagie, Robert A Britton, Jean-Michel Jault
Interactions of an essential Bacillus subtilis GTPase, YsxC, with ribosomes.
J Bacteriol: 2008, 190(2);681-90
[PubMed:17981968]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
K J Boor, M L Duncan, C W Price
Genetic and transcriptional organization of the region encoding the beta subunit of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(35);20329-36
[PubMed:7657605]
[WorldCat.org]
[DOI]
(P p)
