ID   SYL_FRATT               Reviewed;         813 AA.
AC   Q5NG64;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=FTT_0990;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45623.1; -; Genomic_DNA.
DR   RefSeq; WP_003021076.1; NZ_CP010290.1.
DR   RefSeq; YP_169978.1; NC_006570.2.
DR   AlphaFoldDB; Q5NG64; -.
DR   SMR; Q5NG64; -.
DR   STRING; 177416.FTT_0990; -.
DR   DNASU; 3190983; -.
DR   EnsemblBacteria; CAG45623; CAG45623; FTT_0990.
DR   KEGG; ftu:FTT_0990; -.
DR   eggNOG; COG0495; Bacteria.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001174; 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; 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; Reference proteome.
FT   CHAIN           1..813
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152017"
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;  93431 MW;  29E41625623E3548 CRC64;
     MNEYNFSDIE KSTQEYWRKN DTFKTIEDNT KEKFYCLSML PYPSGTLHMG HVRNYTIGDV
     IARYQKMQGK NVLHPMGWDA FGLPAENAAI KHKKSPYEWT KSNIAYMRSQ FDSLGFSFDW
     SREITTCDED 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 KYLTEQNKGY ETTNFRIHDW
     GISRQRYWGC PIPMIHCDDC GAVPEKEENL PVRLPTDVAL TEAGSPLKDI PEFINVACPE
     CGKPAKRETD TFDTFFESSW YYARYTCPTA NQMLDQEANY WLPVDKYIGG IEHAIMHLLY
     ARFFHKLMRD QGLVKSDEPF KNLLTQGMVL KDGAKMSKSK GNIVDPQELI DKYGADTVRL
     FSMFAAPPEQ SLEWSETGVE GANKFLRKVF NYAELNKVIF AKNITLESQK LTKEDKKARF
     EIHSNLKQAI FDFDKSQFNT VVSACMKILN TLNNYDNLSE SVKVEGFSIL LRILAPFTPH
     LCHYLWQQLN LGEDILHTSF PTVDNNALEK DEFLLVVQIN GKLKAKLELD ASLSSNQVEE
     VVLADEHVKS FIDNKQVVKV IYVPQKLINI VIK