ID   SYL_FRAP2               Reviewed;         813 AA.
AC   B0U0E8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
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};
GN   OrderedLocusNames=Fphi_1752;
OS   Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS   O#319-036).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=484022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25017 / FSC 153 / O#319-036;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Richardson P.;
RT   "Complete sequence of chromosome of Francisella philomiragia subsp.
RT   philomiragia ATCC 25017.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000937; ABZ87978.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0U0E8; -.
DR   SMR; B0U0E8; -.
DR   KEGG; fph:Fphi_1752; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_1000074834"
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;  93274 MW;  1BEAB571428237E2 CRC64;
     MSEYNFTQIE QQAQEYWREN NSFKAVEDKN KEKFYCLSML PYPSGTLHMG HVRNYTIGDV
     IARYQKMQGK NVLHPMGWDA FGLPAENAAI KHKKSPYEWT KSNIAYMRSQ LDSLGFSFDW
     SREVATCDES YYKWEQWFFI QLYKKGLAYR KNSVVNWDPV DQTVLANEQV VDGRGWRSGA
     LIEKKEIPQW FLKITDYADE LLKDINQLDG WPEAVKTMQT NWIGKSKGLT VKFKIQNSDK
     EIEVFTTRPD TLMGVSYLGI APEHPLALEE AKTNSQLKSF IDECKRISTM EADLATQEKK
     GFKTSIQAIH PISGETVNVW VANFVLMGYG SGAVMSVPAH DQRDWEFAQK YNIALKQVIK
     PSDNKSKLDL DKEAFTEKGI LINSGEFDGL NFKSAYQAIK KYLFDNDKGY ETTNFRIHDW
     GISRQRYWGC PIPMIHCNDC GLVPEKEENL PVKLPTNVTL TEAGSPLKDI PEFLNVACPN
     CGKPATRETD TFDTFFESSW YYARYTCPTA DKMLSEEANY WLPVDKYIGG IEHAIMHLLY
     ARFFHKLMRD QGLVTSDEPF KNLLTQGMVL KDGAKMSKSK GNTVDPQELI DKYGADTVRL
     FSMFAAPPEQ SLEWSDTGVD GANKFLRKVY NYAYTNKEIL AKNITIDVTK LSKNDKKARY
     EIYANLKQAI FDFDKSQFNT VVSACMKILN TLNNYDNLSD SVKLEGFSIL LRILSPFTPH
     ICHYLWQEIG LGEDILHTQF PTVDDIALEK DEFLLVVQIN GKVKVKLELD ASLTKEQVEQ
     EVLSDEQIKT FIKDKQIVKV IYVPQKLINI VVK
//