ID   SYL_FRATF               Reviewed;         813 AA.
AC   A7NCQ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=FTA_1281;
OS   Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=458234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FTNF002-00 / FTA;
RX   PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA   Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA   Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA   Lion C., Dempsey M.P.;
RT   "Complete genome sequence of Francisella tularensis subspecies holarctica
RT   FTNF002-00.";
RL   PLoS ONE 4:E7041-E7041(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; CP000803; ABU61756.1; -; Genomic_DNA.
DR   RefSeq; WP_003016304.1; NC_009749.1.
DR   AlphaFoldDB; A7NCQ3; -.
DR   SMR; A7NCQ3; -.
DR   KEGG; fta:FTA_1281; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
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; 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; 2.
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..813
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009341"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           575..579
FT                   /note="'KMSKS' region"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   813 AA;  93406 MW;  9B62B05E34D0E689 CRC64;
     MNEYNFSDIE KSTQEYWRKN DTFKTIEDNT KEKFYCLSML PYPSGTLHMG HVRNYTIGDV
     IARYQKMQGK NVLHPMGWDA FGLPAENAAI KHKKSPYEWT KSNIAYMRSQ FDSLGFSFDW
     SREIATCDED YYKWEQWFFI QLYKKGLAYR KNSVVNWDPV DQTVLANEQV VDGRGWRSGA
     LVEKKEIPQW FLKITDYADE LLQDINKLDN WPEAVKTMQI NWIGKSKGLT VKFKVKDSNQ
     EIEVFTTRPD TLMGVNYLGI APEHPLALKE AKSNSQLAAF IEECKKTSTM EADLATQEKK
     GFKTSIKVIH PISAETIDVW VANFVLMGYG SGAVMSVPAH DQRDWEFAQK YNIPLKQVIE
     SNDNKLKIDL EKQAFTEKGI LINSGEFDGL NFKNAYQAIK KYLTKQNKGY ETTNFRIHDW
     GISRQRYWGC PIPMIHCDDC GAVPEKEENL PVRLPTDVAL TEAGSPLKDI PEFINVACPE
     CGKPAKRETD TFDTFFESSW YYARYTCPTS NQMLDQEANY WLPVDKYIGG IEHAIMHLLY
     ARFFHKLMRD QGLVKSDEPF KNLLTQGMVL KDGAKMSKSK GNIVDPQELI DKYGADTVRL
     FSMFAASPEQ SLEWSETGVE GANKFLRKVF NYAELNKVIF AKNITLESQK LTKEDKKARF
     EIHSNLKQAI FDFDKSQFNT VVSACMKILN TLNNYDNLSE SVKVEGFSIL LRILAPFTPH
     LCHYLWQQLN LGEDILHTSF PTVDNNALEK DEFLLVVQIN GKLKAKLELD ASLSSNQVEE
     VVLADEHVKS FIDNKQVVKV IYVPQKLINI VIK