ID SYL_MYCBO Reviewed; 969 AA. AC P67511; A0A1R3XU37; P71698; X2BDV0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=BQ2027_MB0042; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl- CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA- CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00049}. 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; LT708304; SIT98402.1; -; Genomic_DNA. DR RefSeq; NP_853711.1; NC_002945.3. DR RefSeq; WP_003900794.1; NC_002945.4. DR AlphaFoldDB; P67511; -. DR SMR; P67511; -. DR GeneID; 45424000; -. DR PATRIC; fig|233413.5.peg.48; -. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1. DR Gene3D; 3.40.50.620; HUPs; 3. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR NCBIfam; TIGR00396; leuS_bact; 1. DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..969 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000152043" FT MOTIF 78..89 FT /note="'HIGH' region" FT MOTIF 739..743 FT /note="'KMSKS' region" FT BINDING 742 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 969 AA; 107595 MW; A07C835FC1B428D8 CRC64; MTESPTAGPG GVPRADDADS DVPRYRYTAE LAARLERTWQ ENWARLGTFN VPNPVGSLAP PDGAAVPDDK LFVQDMFPYP SGEGLHVGHP LGYIATDVYA RYFRMVGRNV LHALGFDAFG LPAEQYAVQT GTHPRTRTEA NVVNFRRQLG RLGFGHDSRR SFSTTDVDFY RWTQWIFLQI YNAWFDTTAN KARPISELVA EFESGARCLD GGRDWAKLTA GERADVIDEY RLVYRADSLV NWCPGLGTVL ANEEVTADGR SDRGNFPVFR KRLRQWMMRI TAYADRLLDD LDVLDWPEQV KTMQRNWIGR STGAVALFSA RAASDDGFEV DIEVFTTRPD TLFGATYLVL APEHDLVDEL VAASWPAGVN PLWTYGGGTP GEAIAAYRRA IAAKSDLERQ ESREKTGVFL GSYAINPANG EPVPIFIADY VLAGYGTGAI MAVPGHDQRD WDFARAFGLP IVEVIAGGNI SESAYTGDGI LVNSDYLNGM SVPAAKRAIV DRLESAGRGR ARIEFKLRDW LFARQRYWGE PFPIVYDSDG RPHALDEAAL PVELPDVPDY SPVLFDPDDA DSEPSPPLAK ATEWVHVDLD LGDGLKPYSR DTNVMPQWAG SSWYELRYTD PHNSERFCAK ENEAYWMGPR PAEHGPDDPG GVDLYVGGAE HAVLHLLYSR FWHKVLYDLG HVSSREPYRR LVNQGYIQAY AYTDARGSYV PAEQVIERGD RFVYPGPDGE VEVFQEFGKI GKSLKNSVSP DEICDAYGAD TLRVYEMSMG PLEASRPWAT KDVVGAYRFL QRVWRLVVDE HTGETRVADG VELDIDTLRA LHRTIVGVSE DFAALRNNTA TAKLIEYTNH LTKKHRDAVP RAAVEPLVQM LAPLAPHIAE ELWLRLGNTT SLAHGPFPKA DAAYLVDETV EYPVQVNGKV RGRVVVAADT DEETLKAAVL TDEKVQAFLA GATPRKVIVV AGRLVNLVI //