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 18-SEP-2019, entry version 73. 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; OC 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 RT erythropolis 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 CC and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to CC membrane-bound phosphatidylglycerol (PG), which produces CC lysylphosphatidylglycerol (LPG), one of the components of the CC bacterial membrane with a positive net charge. LPG synthesis CC contributes to the resistance to cationic antimicrobial peptides CC (CAMPs) and likely protects M.tuberculosis against the CAMPs CC produced by competiting microorganisms (bacteriocins). In fact, CC the modification of anionic phosphatidylglycerol with positively CC charged L-lysine results in repulsion of the peptides (By CC 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, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, CC ChEBI:CHEBI:456215; EC=6.1.1.6; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L- CC lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L- CC lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA- CC COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, CC ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; CC 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 CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the LPG CC synthetase 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 SMR; C1B7Z5; -. DR PRIDE; C1B7Z5; -. DR EnsemblBacteria; BAH51798; BAH51798; ROP_35510. DR KEGG; rop:ROP_35510; -. DR PATRIC; fig|632772.20.peg.3720; -. DR eggNOG; ENOG4105CRK; Bacteria. DR eggNOG; COG1190; LUCA. DR eggNOG; COG2898; LUCA. DR HOGENOM; HOG000046227; -. DR KO; K04567; -. DR OMA; WDLVAFG; -. DR OrthoDB; 63621at2; -. DR Proteomes; UP000002212; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 HAMAP; MF_00252; Lys_tRNA_synth_class2; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR024320; LPG_synthase_C. DR InterPro; IPR002313; Lys-tRNA-ligase_II. 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; DUF2156; 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; SSF50249; SSF50249; 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; Complete proteome; DNA-binding; Ligase; KW Lipid metabolism; Magnesium; Membrane; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 1114 Lysylphosphatidylglycerol biosynthesis FT bifunctional protein LysX. FT /FTId=PRO_0000394335. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT DNA_BIND 674 751 OB. FT REGION 1 618 Phosphatidylglycerol lysyltransferase. FT REGION 619 1114 Lysine--tRNA ligase. FT METAL 1025 1025 Magnesium 1. {ECO:0000250}. FT METAL 1032 1032 Magnesium 1. {ECO:0000250}. FT METAL 1032 1032 Magnesium 2. {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 //