ID   SYL_FRATM               Reviewed;         813 AA.
AC   B2SGM9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=FTM_0959;
OS   Francisella tularensis subsp. mediasiatica (strain FSC147).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=441952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC147;
RX   PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA   Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA   Keim P., Johansson A.;
RT   "Molecular evolutionary consequences of niche restriction in Francisella
RT   tularensis, a facultative intracellular pathogen.";
RL   PLoS Pathog. 5:E1000472-E1000472(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; CP000915; ACD30888.1; -; Genomic_DNA.
DR   RefSeq; WP_012429522.1; NC_010677.1.
DR   AlphaFoldDB; B2SGM9; -.
DR   SMR; B2SGM9; -.
DR   KEGG; ftm:FTM_0959; -.
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_1000091320"
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;  93519 MW;  5AB1688851684D2E 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 AKSNSQLAEF IEECKKTSTM EADLATQEKK
     GFKTSIKVIH PISAETIDVW VANFVLMGYG SGAVMSVPAH DQRDWEFAQK YNIPLKQVIE
     SNDNKLKIDL EKQAFTEKGI LINSGEFDSL NFKNAYQAIK KYLTEQNKGY ETTNFRIHDW
     GISRQRYWGC PIPMIHCDDC GAVPEKEENL PVRLPTDVAL TEAGSPLKDI PEFINVACPE
     CGKPAKRETD TFDTFFESSW YYARYTCPTA NQMLDQEANY WLPVDKYIGG IEHAIMHLLY
     ARFFHKLMRD QGLVKSDEPF KNLLTQGMVL KDGAKMSKSK GNIVDPQELI DKYGADTVRL
     FSMFAAPPEQ SLEWSETGVE GTNKFLRKVF NYAELNKVIF AKNITLESQK LTKEDKKARF
     EIHSNLKQAI FDFDKSQFNT VVSACMKILN TLNNYDNLSE SVKVEGFSIL LRILAPFTPH
     LCHYLWQQLN LGEDILHTSF PTVDNNALEK DEFLLVVQIN GKLKAKLELD ASLSSNQVEE
     VVLADEHVKS FIDNKQVVKV IYVPQKLINI VIK