Difference between revisions of "RpmGA"
| Line 1: | Line 1: | ||
| − | * '''Description:''' [[ribosomal protein]] | + | * '''Description:''' [[ribosomal protein]] L33a <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 79: | Line 79: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
** phosphorylated on Arg-29 {{PubMed|22517742}} | ** phosphorylated on Arg-29 {{PubMed|22517742}} | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| Line 103: | Line 103: | ||
=== Additional information=== | === Additional information=== | ||
| − | * the protein is significantly underrepresented in 45S assembly intermediates that accumulate upon depletion of [[RbgA]] {{PubMed|23700310}} | + | * the protein is significantly underrepresented in 45S assembly intermediates that accumulate upon depletion of [[RbgA]] {{PubMed|24335279,23700310}} |
=Expression and regulation= | =Expression and regulation= | ||
| Line 138: | Line 138: | ||
=References= | =References= | ||
| − | <pubmed> 19648245 22517742 23002217 23700310</pubmed> | + | <pubmed> 19648245 22517742 23002217 24335279,23700310</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 17:24, 18 December 2013
- Description: ribosomal protein L33a
| Gene name | rpmGA |
| Synonyms | |
| Essential | no PubMed |
| Product | ribosomal protein L33a |
| Function | translation |
| Gene expression levels in SubtiExpress: rpmGA | |
| Interactions involving this protein in SubtInteract: RpmGA | |
| MW, pI | 5 kDa, 10.436 |
| Gene length, protein length | 147 bp, 49 aa |
| Immediate neighbours | yqgN, yqgM |
| 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
The gene
Basic information
- Locus tag: BSU24900
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 L33P family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- phosphorylated on Arg-29 PubMed
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P56849
- KEGG entry: [2]
- E.C. number:
Additional information
- the protein is significantly underrepresented in 45S assembly intermediates that accumulate upon depletion of RbgA PubMed
Expression and regulation
- Operon:
- Regulation:
- 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
Ahmad Jomaa, Nikhil Jain, Joseph H Davis, James R Williamson, Robert A Britton, Joaquin Ortega
Functional domains of the 50S subunit mature late in the assembly process.
Nucleic Acids Res: 2014, 42(5);3419-35
[PubMed:24335279]
[WorldCat.org]
[DOI]
(I p)
Ningning Li, Yuling Chen, Qiang Guo, Yixiao Zhang, Yi Yuan, Chengying Ma, Haiteng Deng, Jianlin Lei, Ning Gao
Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.
Nucleic Acids Res: 2013, 41(14);7073-83
[PubMed:23700310]
[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)
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)
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)
