ID A0AAC9AN68_9ACTN Unreviewed; 1081 AA. AC A0AAC9AN68; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 05-FEB-2025, entry version 5. DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252}; DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252}; DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252}; DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252}; GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252}; GN ORFNames=AXH35_04755 {ECO:0000313|EMBL:AMS04886.1}; OS Acidipropionibacterium acidipropionici. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales; OC Propionibacteriaceae; Acidipropionibacterium. OX NCBI_TaxID=1748 {ECO:0000313|EMBL:AMS04886.1, ECO:0000313|Proteomes:UP000075221}; RN [1] {ECO:0000313|EMBL:AMS04886.1, ECO:0000313|Proteomes:UP000075221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55737 {ECO:0000313|EMBL:AMS04886.1, RC ECO:0000313|Proteomes:UP000075221}; RA Luna Flores C.H., Nielsen L.K., Marcellin E.; RT "Complete Genome Sequence of Propionibacterium acidipropionici ATCC RT 55737."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the CC transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound CC phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol CC (LPG), one of the components of the bacterial membrane with a positive CC net charge. LPG synthesis contributes to the resistance to cationic CC antimicrobial peptides (CAMPs) and likely protects M.tuberculosis CC against the CAMPs produced by competiting microorganisms CC (bacteriocins). In fact, the modification of anionic CC phosphatidylglycerol with positively charged L-lysine results in CC repulsion of the peptides. {ECO:0000256|ARBA:ARBA00024681}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-tRNA(Lys) + a 1,2-diacyl-sn-glycero-3-phospho-(1'-sn- CC glycerol) = a 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn- CC glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, CC Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3; CC Evidence={ECO:0000256|ARBA:ARBA00047540}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Lys) + L-lysine + ATP = L-lysyl-tRNA(Lys) + AMP + CC diphosphate; Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA- CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CC Evidence={ECO:0000256|ARBA:ARBA00048573, ECO:0000256|HAMAP- CC Rule:MF_00252}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00252}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00252}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II CC aminoacyl-tRNA synthetase family. {ECO:0000256|ARBA:ARBA00009968}. CC -!- SIMILARITY: In the N-terminal section; belongs to the LPG synthetase CC family. {ECO:0000256|ARBA:ARBA00005270}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP014352; AMS04886.1; -; Genomic_DNA. DR RefSeq; WP_062819224.1; NZ_CP031057.1. DR Proteomes; UP000075221; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0000049; F:tRNA binding; IEA:TreeGrafter. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR CDD; cd04322; LysRS_N; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1. DR InterPro; IPR004364; Aa-tRNA-synt_II. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR024320; LPG_synthase_C. DR InterPro; IPR002313; Lys-tRNA-ligase_II. DR InterPro; IPR044136; Lys-tRNA-ligase_II_N. DR InterPro; IPR018149; Lys-tRNA-synth_II_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR InterPro; IPR031553; tRNA-synt_2_TM. DR NCBIfam; TIGR00499; lysS_bact; 1. DR PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL; 1. DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1. DR Pfam; PF09924; LPG_synthase_C; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF16995; tRNA-synt_2_TM; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR00982; TRNASYNTHLYS. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00252}; KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00252}; Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00252}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 25..48 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 60..82 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 102..123 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 135..156 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 755..1077 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT BINDING 990 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" FT BINDING 997 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" FT BINDING 997 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" SQ SEQUENCE 1081 AA; 117795 MW; 41737D41C53FDE11 CRC64; MLVGAVLLIG RMLFQQTWWV SALATGFSIV VFPIDGGGWG LVVLLLILAA GLNRRKRLSW AVCLGLFGLM WVVSLLFFGV LIAEVAGGEP TRIHDDVEMA GYVFNTFSVG AILVALIVHH GRFGARTARA NVRPALATLV GGLAATVLIG WLLVWATGGQ GRPRNRLWRL ISELLRGNRS QVAPPSPIWV ENIVELLAAI TLATAFIMLL RSQRQVAVLG LGDELELRNL LDENPSDSLG YFALRRDKAV VFSPDRRAAV CYRAVAGVAL ASGDPVGPRA QWPAAIDAFL TVAHTYGWSP AVVGASEEGA TAWQGAGLRV TRIGDEAIIS PSTFDLQSRD LRGVRSVVNR LRRSGYTVRV RRHSDIEPDE LSRLIALADA WRADGEERGF SMALSRLGDP LDGDCVMVEA LYPAGDIRGD GSTAGLLSFV PWGGDGLSLD VMRHDPRADN GVTELMVAGL MATGRELGLH RVSLNFAVFR EVIEEGSRVG ARPLQRLAAR FVSGVSRWFQ IEQLYRSNVK YAPDWQARYL GYADAGELAQ VGLALGLAEG QIDLPRILRP APPPAQPIYS VAAHPEIAAV LERQRPDVEL PGRRVGEQMR HRQQTRERII AAGGEAYPPD IHPSGAPGDL ATAAEGGELS LVGRVAGVRD HGGVIFADLT DWSGTAQILL DASALGAPAM DRWRADISLG DHVLVGGRAG SSRNGTRSLL AGEFRLAAKA LHPLPDRRSG MSDPEEKVRR RYLDLIVNPA ARDELRARSQ AIRAVRETLL SHDFLEVETP ILQTIHGGAN ARPFRTHINA YDLDLYLRIA PELYLKRLMV GGAGRVFEIG RNFRNEGADA THNPEFTMLE AYQAYGDYVQ MRHLTREMIL AASRRATGGT VIHGRDADGV EHEMDLAEEW RVITVNEGIS AALGEEVTAD TPKETLVGYA EKLGIAVSPK WDRGDVVLEL HEHLSERTTV GPTFFCDFPA DVSPLTRQHR DDPRLAEKWD LIVLGDEVAT AYTELVDPVI QRERFTAQSL RAAGGDPEAM ELDEDFLEAL EYAMPPTGGM GMGLDRLVML LTGASIRQTI TFPLVRPRSS S //