Difference between revisions of "LysS"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3E9I 2E9I] (from ''Geobacillus stearothermophilus'', in complex with L-Lysine hydroxamate-AMP) {{PubMed|19174549}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37477 P37477] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37477 P37477] |
Revision as of 19:21, 16 August 2009
- Description: lysyl-tRNA synthetase
Gene name | lysS |
Synonyms | |
Essential | yes PubMed |
Product | lysyl-tRNA synthetase |
Function | translation |
Metabolic function and regulation of this protein in SubtiPathways: tRNA charging, Folate | |
MW, pI | 57 kDa, 5.034 |
Gene length, protein length | 1497 bp, 499 aa |
Immediate neighbours | yacF, rrnJ-16S |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU00820
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) (according to Swiss-Prot)
- Protein family: class-II aminoacyl-tRNA synthetase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 2E9I (from Geobacillus stearothermophilus, in complex with L-Lysine hydroxamate-AMP) PubMed
- UniProt: P37477
- KEGG entry: [3]
- E.C. number: 6.1.1.6
Additional information
Expression and regulation
lysS PubMed
- 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
Antoine de Saizieu, Pierre Vankan, Cassandra Vockler, Adolphus P G M van Loon
The trp RNA-binding attenuation protein (TRAP) regulates the steady-state levels of transcripts of the Bacillus subtilis folate operon.
Microbiology (Reading): 1997, 143 ( Pt 3);979-989
[PubMed:9084182]
[WorldCat.org]
[DOI]
(P p)