A0A6N7CWG9 · A0A6N7CWG9_9NOCA
- ProteinLysine--tRNA ligase
- GenelysX
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1113 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides.
Catalytic activity
- 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | lysine-tRNA ligase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | nucleic acid binding | |
Molecular Function | phosphatidylglycerol lysyltransferase activity | |
Biological Process | lipid metabolic process | |
Biological Process | lysyl-tRNA aminoacylation | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLysine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus
Accessions
- Primary accessionA0A6N7CWG9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 37-60 | Helical | ||||
Sequence: IAGLILGVFSVLVFLWSISPVLRY | ||||||
Transmembrane | 80-95 | Helical | ||||
Sequence: SLSWALVVALLAAALA | ||||||
Transmembrane | 102-122 | Helical | ||||
Sequence: WWLLTIYLTLILITNVIVSIT | ||||||
Transmembrane | 128-145 | Helical | ||||
Sequence: AMVAAVVQVVLIGILIAA | ||||||
Transmembrane | 157-180 | Helical | ||||
Sequence: AGWKALGVLIVGLAIGTLVGWGLV | ||||||
Transmembrane | 218-239 | Helical | ||||
Sequence: FVNTLLGLFGALALLAAVITLF |
Keywords
- Cellular component
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MSASTETHHASEADLTAPRPR | ||||||
Domain | 792-1111 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: RSAVVKSLRDSLGGRGFLEVETPILQQVHGGANAAPFLTHINAYNLDLYLRIAPELYLKRLCVAGMEKVFEIGRVFRNEGVDFKHNPEFTILEAYEAHSDYEKMMVLCRELIQTAAVAAYGREIIMRPGPDGRLVEVDISGEWPVKTMHQAVAEKLGVDVSPETPLAELQRLCDEHEIPYQSAWDAGAVAQEMYEHLVEDYTEFPTFYTNFPTSMSPLTRPHPTIPGVAAKWDLVAWGIELGTAYSELTDPVDQRNRLTEQSMLAAGGDEEAMELDEDFLQALEHAMPPTGGLGMGVDRVVMLITGGSIRETLAFPLAKP |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.
In the N-terminal section; belongs to the LPG synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,113
- Mass (Da)122,294
- Last updated2020-10-07 v1
- ChecksumF58C83C0F077E6E0
Keywords
- Technical term