ID   SYL_MYCBT               Reviewed;         969 AA.
AC   C1AJ38;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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}; OrderedLocusNames=JTY_0042;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(2009).
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}.
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DR   EMBL; AP010918; BAH24343.1; -; Genomic_DNA.
DR   RefSeq; WP_003900794.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1AJ38; -.
DR   SMR; C1AJ38; -.
DR   GeneID; 45424000; -.
DR   KEGG; mbt:JTY_0042; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
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   Gene3D; 3.40.50.620; -; 3.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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.
FT   CHAIN           1..969
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199215"
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