ID   SYL_MYCLB               Reviewed;         972 AA.
AC   B8ZTR5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=MLBr00032;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(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; FM211192; CAR70125.1; -; Genomic_DNA.
DR   RefSeq; WP_010907481.1; NC_011896.1.
DR   AlphaFoldDB; B8ZTR5; -.
DR   SMR; B8ZTR5; -.
DR   EnsemblBacteria; CAR70125; CAR70125; MLBr00032.
DR   KEGG; mlb:MLBr00032; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006900; 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; -; 2.
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..972
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199216"
FT   MOTIF           78..89
FT                   /note="'HIGH' region"
FT   MOTIF           741..745
FT                   /note="'KMSKS' region"
FT   BINDING         744
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   972 AA;  108408 MW;  65286839DA51AFAE CRC64;
     MTELPTTVPG YNSAVAQTDS DAMRYRYTAE LAGRIESTWQ DNWARLQTFN VPNPVGSLAP
     PDGSVVPADK LFVQDMFPYP SGDGLHVGHP LGYIATDVYA RYFRMTGHNV LHAMGFDAFG
     LPAEQYAMQT GTHPRILTEA NVVNFRHQLG RLGLGHDSRR TFSTTDVEFY KWTQWIFLQI
     YNAWFDVAAN KARPIAELIA EFDSGERRLV DGRDWATLSA GERADVIDNC RLVYRADSMV
     NWCPGLGTVL ANEEVTADGR SDRGNFPVFR KRLRQWMMRI TAYADRLLDD LDLLDWPEQV
     KTMQRNWIGR SSGATVLFSA ILSRSDAATT EVDVEVFTTR PDTMFGVTYL VLAPEHNLVD
     ELVATVWPDR TDPRWTYGAA TPGAAVAAYR RAIVAKSDLD RQESKEKTGV FLGRYATNPA
     TGKPVPIFVA DYVLVGYGTG AVMAVPGHDP RDWDFAHKFH LPIVEVIAGS DISEAAYVGD
     GVLVNSGYLD GMDVATAQEA ITARLESEGR GHARIEFKLR DWLFARQRYW GEPFPIIYDS
     DGRPHALDEA ALPVELPDVP YYSPVLFDPD DADSEPSPPL AKATEWVHVE LDLGDGLKPY
     SRDTNVMPQW AGSSWYELRY TDPHNSERLC AKENEAYWMG PRPTEHGIDD PGGVDLYVGG
     AEHAVLHLLY ARFWHKVLYD LGHVSSREPY RRLINQGYIQ AFAYTDAHGS YVPANQVFQR
     GDGFFCPGPD GEIEVFQEFG KIGKSLKNSV SPDEICDEYG ADTLRVYEMS MGPLEASRPW
     ATKDVVGAYR FLQRVWRLVV DERTGETRVV DTAGELDTYT LRTLHRTIAG VSQDYAALRN
     NTATAKLIEY TNHLTKEHRG SVPRVAVEPL VLMLAPLAPH LAEELWLRLG HTTSLANGPF
     PQADPAYLVD DTVEYPVQVN GKIRGRIVVA ADADYDTLKT VALADDKVQQ FLAGATPRKV
     IVVAGRLISL VI