ID   SYL_MYCTO               Reviewed;         969 AA.
AC   P9WFV0; L0T451; P67510; P71698;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=MT0047;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44269.1; -; Genomic_DNA.
DR   PIR; A70912; A70912.
DR   RefSeq; WP_003900794.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFV0; -.
DR   SMR; P9WFV0; -.
DR   EnsemblBacteria; AAK44269; AAK44269; MT0047.
DR   GeneID; 45424000; -.
DR   KEGG; mtc:MT0047; -.
DR   PATRIC; fig|83331.31.peg.46; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000001020; 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   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_0000428473"
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