Application | Comment | Organism |
---|---|---|
drug development | aminoacyl-tRNA synthetases are attractive targets for the discovery of antibacterial agents | Mycolicibacterium smegmatis |
Cloned (Comment) | Organism |
---|---|
gene lysS, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in conditional expression strains of Mycobacterium smegmatis strain mc2155 | Mycolicibacterium smegmatis |
gene lysS2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in conditional expression strains of Mycobacterium smegmatis | Mycolicibacterium smegmatis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview | Mycolicibacterium smegmatis |
additional information | generation of conditional expression strains, conditional expression plasmids are electroporated intoMycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview | Mycolicibacterium smegmatis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | transmembrane segment analysis of lysyl-tRNA synthetase | Mycolicibacterium smegmatis | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Mycolicibacterium smegmatis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-lysine + tRNALys | Mycolicibacterium smegmatis | - |
AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
ATP + L-lysine + tRNALys | Mycolicibacterium smegmatis mc2155 / ATCC 700084 | - |
AMP + diphosphate + L-lysyl-tRNALys | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | A0QYV1 | gene lysX or lysS2 | - |
Mycolicibacterium smegmatis | A0R577 | gene lysS | - |
Mycolicibacterium smegmatis mc2155 / ATCC 700084 | A0QYV1 | gene lysX or lysS2 | - |
Mycolicibacterium smegmatis mc2155 / ATCC 700084 | A0R577 | gene lysS | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-lysine + tRNALys | - |
Mycolicibacterium smegmatis | AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
ATP + L-lysine + tRNALys | - |
Mycolicibacterium smegmatis mc2155 / ATCC 700084 | AMP + diphosphate + L-lysyl-tRNALys | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LysRS | - |
Mycolicibacterium smegmatis |
lysS | - |
Mycolicibacterium smegmatis |
lysS2 | - |
Mycolicibacterium smegmatis |
LysX | - |
Mycolicibacterium smegmatis |
LysX | UniProt | Mycolicibacterium smegmatis |
Lysyl-tRNA synthetase | - |
Mycolicibacterium smegmatis |
lysylphosphatidylglycerol biosynthesis bifunctional protein | UniProt | Mycolicibacterium smegmatis |
MSMEG_3796 | - |
Mycolicibacterium smegmatis |
MSMEG_6094 | - |
Mycolicibacterium smegmatis |
MSMEI_3707 | - |
Mycolicibacterium smegmatis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mycolicibacterium smegmatis |
General Information | Comment | Organism |
---|---|---|
evolution | multiple genes encode for aminoacyl-tRNA synthetases from Mycobacterium smegmatis, e.g. glutamyl (GluRS), cysteinyl (CysRS), prolyl (ProRS) and lysyl (LysRS) tRNA synthetases. Conditional expression strains of lysyl-tRNA synthetases generated in Mycobacterium smegmatis reveals that the canonical aminoacyl-tRNA synthetase are essential, while the additional ones are not essential for the growth of Mycobacterium smegmatis. The lysyl-tRNA synthetase of Mycobacterium smegmatis belongs to the class II amino acid tRNA synthetases | Mycolicibacterium smegmatis |
physiological function | canonical LysRS and CysRS are essential for growth of Mycobacterium smegmatis | Mycolicibacterium smegmatis |
physiological function | Essentiality of lysyl and cysteinyl-tRNA synthetases of Mycobacterium smegmatis | Mycolicibacterium smegmatis |