ID   SYL_BUCAP               Reviewed;         861 AA.
AC   Q8K9B9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=BUsg_429;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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}.
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DR   EMBL; AE013218; AAM67972.1; -; Genomic_DNA.
DR   RefSeq; WP_011053939.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9B9; -.
DR   SMR; Q8K9B9; -.
DR   STRING; 198804.BUsg_429; -.
DR   PRIDE; Q8K9B9; -.
DR   EnsemblBacteria; AAM67972; AAM67972; BUsg_429.
DR   KEGG; bas:BUsg_429; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000416; 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   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; 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; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151988"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  102107 MW;  3616484C35A366E0 CRC64;
     MEKEYCPKNI EPYVQQYWKD NKVFHVYEDD KKEKYYCLPM LPYPSGKLHM GHVRNYTISD
     VISRYQRMLG KNVLQPIGWD AFGLPAEEAA IKNKTKPSDW TQKNIKYMKK QLQSLGFSYD
     WSREITTCKP DYYCWEQWFF IQLYKKKLVY KKNSFVNWCP YDKTVLANEQ VIKGCCWRCQ
     NKIKVKKIPQ WFIKIRNYAE SLHNDLNDLE NWPEKVKNMQ RNWIGRSKGF EIVFNVLNSN
     KKIKAFTNRL DLIMGATYIS ISPCHEFSVH VSKEKKEIQK FIDQKINNSA SQEDIEKIKF
     EGINSNMFVI HPITNKKIPV WISNFIQKEY GTNAIISVPG HNQNDWNFSI KHNLKIKYVI
     KNKKYKNTQL HNLFTTEKGI LYNSGEFNNL NYHNATEKIK KTLLKKKIIK EKINYKLQDW
     CISRQRYWGT PIPMATKKNG EIIAIPEKNL PVLLPEIKNY SDSLQKPMDS SSKWANIKIE
     NQDVIRETDT FDTFMESSWY YARYTCPNFN TGMIDPTASK YWLPVDQYIG GIEHATMHLI
     YFRFYHKLLR DFKLVELNEP VKNLICQGMV LSEAFYQFDK NNQRNWIHPS CVQVEKNLKG
     ETIKVDIKNK KKVIYAGMIK MSKSKNNGIE PELMINRYGA DTLRLFIMFA APIESSLEWR
     ESGVKGIYRF LKKIWKLVFN HIEVKKINKK VNFDILNKKQ KKMYCLLHKT IIKVSDDIGR
     RKSFNTAISS IMELVNELSI FKIENEEDKS IIKESLMSII KMLYPFTPHF CFRLWQYLNK
     NCCIDYETWP TFEKKILSSD KNTLIIQING KKQCAIEVKN HLNKEEILSY IENQSIIQKK
     IKNLKIIKII YIPQKVINFV V