ID LYSX_RHOOB Reviewed; 1114 AA. AC C1B7Z5; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 14-DEC-2022, entry version 90. DE RecName: Full=Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX; DE Includes: DE RecName: Full=Lysine--tRNA ligase; DE EC=6.1.1.6; DE AltName: Full=Lysyl-tRNA synthetase; DE Short=LysRS; DE Includes: DE RecName: Full=Phosphatidylglycerol lysyltransferase; DE EC=2.3.2.3; DE AltName: Full=Lysylphosphatidylglycerol synthetase; DE Short=LPG synthetase; GN Name=lysX; OrderedLocusNames=ROP_35510; OS Rhodococcus opacus (strain B4). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=632772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus erythropolis RT PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2009) 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 (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl- CC tRNA(Lys); 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 -!- CATALYTIC ACTIVITY: CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl- CC tRNA(Lys) = 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the LPG synthetase CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II CC aminoacyl-tRNA synthetase family. {ECO:0000305}. 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; AP011115; BAH51798.1; -; Genomic_DNA. DR RefSeq; WP_012690737.1; NC_012522.1. DR AlphaFoldDB; C1B7Z5; -. DR SMR; C1B7Z5; -. DR STRING; 632772.ROP_35510; -. DR EnsemblBacteria; BAH51798; BAH51798; ROP_35510. DR KEGG; rop:ROP_35510; -. DR PATRIC; fig|632772.20.peg.3720; -. DR HOGENOM; CLU_008255_2_0_11; -. DR OMA; DISGEWP; -. DR OrthoDB; 63621at2; -. DR Proteomes; UP000002212; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050071; F:lysyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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; 2.40.50.140; -; 1. DR Gene3D; 3.30.930.10; -; 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 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 TIGRFAMs; TIGR00499; lysS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; Antibiotic resistance; ATP-binding; KW Cell membrane; DNA-binding; Ligase; Lipid metabolism; Magnesium; Membrane; KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..1114 FT /note="Lysylphosphatidylglycerol biosynthesis bifunctional FT protein LysX" FT /id="PRO_0000394335" FT TRANSMEM 38..58 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 77..97 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 101..121 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255" FT DNA_BIND 674..751 FT /note="OB" FT REGION 1..618 FT /note="Phosphatidylglycerol lysyltransferase" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 619..1114 FT /note="Lysine--tRNA ligase" FT BINDING 1025 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 1032 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 1032 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 1114 AA; 122292 MW; BAE0618F5814EB62 CRC64; MSASTETHHA SEAAVPTAPR PRPALGSKSG RLHQVPHIAG LILGVFSVLV FLWSISPVLR YYVHVPREYI DTYYFDAPDT SLSWALVVAL LAAALASRKR IAWWLLTIYL VLILITNVIV SITDRNVNAM VAAVVQVVLI GILVAARPEF YTRVRRGAGW KALGVLIVGL AIGTLVGWGL VELFPGTLPQ GERFLWALNR VTALAAADNE QFSGRPHGFV NTLLGLFGAM ALLAAVITLF RAQRSHNALT GNDESALRGL LLQYGADDSL GYFATRRDKA VVFAPSGKAA ITYRVELGVC LASGDPIGDP EAWPHAIEAW QTLASQYGWA TAVMGASETG ATAYNKAGLT VLQLGDEAIL RTREFNLSGR DMRQVRQAVT RVRRQGVTVR IRRHRDVPPE EMAEAIRLAD AWRDTETERG FSMALGRLGD RLDGDCLLVE AIAEDGEIDG ILSLVPWGPT GVSLDLMRRK PTSPNGVVEL MVSELATTSD QFGITKVSLN FAVFRSVFEE GSRIGAGPIL RIWRSILVFF SRWWQLEALY RSNVKYQPEW VPRFLCFDDN RELLRVGFAS AVAEGFVTLP RFGRSGTHDA IEHTGHHAAV PAALVAAEGL HSDGSAPGEG LAPTATGPKR PEQVRVRLDK LTGLAEQGID PYPVAYPPSH TVTEAVESPE GTTVRIAGRL LRIRDYGGVV FAVVRDWSGD IQVLVDEARV GTDRIRAFAA EFDLGDLVEV AGVIGYSRRG ALSLLANEWR MTGKCLHPLP DKWKGLSDPE TRVRQRYVDL AINTDARRLL EARSAVVKSL RDSLGGRGFL EVETPILQQV HGGANAAPFL THINAYNLDL YLRIAPELYL KRLCVAGMEK VFEIGRVFRN EGVDFKHNPE FTILEAYEAH SDYEKMMVLC RELIQTAAVA AYGREIIMRP GPDGTLVEVD ISGEWPVKTM HQAVAEKLGV DVSPETPLAE LQRLCDEHEI PYQSTWDAGA VAQEMYEHLV EDYTEFPTFY TNFPTSMSPL TRPHPTIPGV AAKWDLVAWG VELGTAYSEL TDPVDQRNRL TEQSMLAAGG DEEAMELDED FLQALEHAMP PTGGLGMGVD RVVMLITGGS IRETLAFPLA KPRQ //