ID   SYL_LIMRJ               Reviewed;         806 AA.
AC   B2G8G2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=LAR_1228;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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; AP007281; BAG25744.1; -; Genomic_DNA.
DR   RefSeq; WP_003668546.1; NC_010609.1.
DR   AlphaFoldDB; B2G8G2; -.
DR   SMR; B2G8G2; -.
DR   GeneID; 66471437; -.
DR   KEGG; lrf:LAR_1228; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
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; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_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..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091330"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           578..582
FT                   /note="'KMSKS' region"
FT   BINDING         581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  92919 MW;  08383790E3207E6C CRC64;
     MAYDHKTIEK KWQKFWKKNE TFKADLNKDQ KKYYALDMFP YPSGQGLHVG HPEGYTATDV
     MSRMKRMQGF NVLHPMGWDA FGLPAEQYAL KTGHNPKDFT NKNIDHFRDQ IQSLGFSYDW
     DREVNTTDPK FYKWTQWIFE QLYKKGLAYE SEIMVNWAPD FMGGTVVANE EVEDGKTKRG
     GYPVYRKPMR QWVLKITAYA DRLIDDLDLV DWPESVKEMQ RNWIGRSEGA SVFFPVVGDE
     DTKIEVFTTR ADTLFGASYV VLAPEQELVD QLTTPEHKAE VEKYKEEASR RSDLERTDLN
     KDKTGVFTGS YVINPVNGEK LPIWISDYVL ASYGTGAVMA VPSGDQRDYD FATKFNLPIK
     PIIEGADISE GAFDGDGKHI NSGFLDGLNI ADAKQKMIDW LEEHDAGHKK VNYRLRDWIF
     SRQRYWGEPI PVIHWDDGTT SLVPEDELPL ELPKTDNIEP SGTGESPLAN VEDWVNVYDE
     NGRHGLRETN TMPQWAGSSW YWLRYTDPHN DEEFASKEAL DYWSPVDLYV GGAEHAVLHL
     LYARFWHKVL YDLGLVPTKE PFMKLVNQGM ILGSNHEKMS KSKGNVVNPD DIVDQYGADT
     LRLYEMFMGP LEESVPWDEK GLHGANKWVQ RVWRLLMDDN NHLRDRVSTF NDGKLTKVYN
     QTVKKVTEDY ERMHFNTAIS QLMVFVNEAY KVDDLPVEYM KGFVKMIAPI MPHMAEELWS
     QFGESDTITY QPWPTYDPKA LVEDEVEMIV QVNGKVRAKI KMAKDTDRDE AQQLALANEH
     VKKFTDGKDI KKVIVVPNKI VNIVAK