Difference between revisions of "RpsI"
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* '''Domains:''' | * '''Domains:''' | ||
− | * '''Modification:''' | + | * '''Modification:''' |
+ | ** phosphorylated on Arg-20 {{PubMed|22517742}} | ||
+ | ** acetylated at the N-terminus {{PubMed|19653700}} | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
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=References= | =References= | ||
− | <pubmed>19653700 </pubmed> | + | <pubmed>19653700 22517742</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 15:11, 21 April 2012
- Description: ribosomal protein
Gene name | rpsI |
Synonyms | |
Essential | yes PubMed |
Product | ribosomal protein S9 |
Function | translation |
Interactions involving this protein in SubtInteract: RpsI | |
MW, pI | 14 kDa, 11.007 |
Gene length, protein length | 390 bp, 130 aa |
Immediate neighbours | rplM, ybaJ |
Get the DNA and protein sequences (Barbe et al., 2009) | |
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: BSU01500
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 S9P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P21470
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
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)