ID   SYL_TROWT               Reviewed;         806 AA.
AC   Q83GC6;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=TWT_385;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC   Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44482.1; -; Genomic_DNA.
DR   RefSeq; WP_011102542.1; NC_004572.3.
DR   AlphaFoldDB; Q83GC6; -.
DR   SMR; Q83GC6; -.
DR   STRING; 203267.TWT_385; -.
DR   KEGG; twh:TWT_385; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002200; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; 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; Reference proteome.
FT   CHAIN           1..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152111"
FT   MOTIF           54..64
FT                   /note="'HIGH' region"
FT   MOTIF           571..575
FT                   /note="'KMSKS' region"
FT   BINDING         574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  92300 MW;  6A6153B7178A397B CRC64;
     MHALRALDTL CENMEYNFRA LEEKWAPIWE RDRLFEVDEN DSETPRKYVL DMFSYPSGDL
     HMGHAETYAY GDFIARYWRH RGYNVLHPVG WDSFGLPAEN AAIKHGSDPK VWTYRNIDQQ
     ARSMRLYAAS FDWSRRLHTS DPEYYRWNQW LFLKLYKHGL AYRKKAWVNW DPSDRTVLAN
     EQVLPDGTSE RSGALVVKKK LTQWFLRITA YADRLLDDLS MLENNWPERV ITMQRNWIGR
     SEGVSIEFNI PTLKRPVTVF TTRPETIFGV TYLALAFDSE VTEELASKSG VLGELLELRH
     NIDKTHEGVR GLDLKSFAIH PLTGQSVPIF AASYILSDYA KGAVMSVPGH DTRDERFAVR
     YNLPIVKIME DNRLISSGKY SGQSVTQARE NITRDLCAKS LGRREISYRL RDWLISRQRY
     WGTPIPILYD SNGSEIPVEE DDLPVLLPDS EGIDLTPSGL SPLGGIHDWV NLHKAGSLFR
     RDTDTMDTFF DSSWYFLRYL NPDCDTAPFT LEKAKKWGPV DQYCGGVEHA VLHLLYARFI
     TKFLYDIGFV DFKEPFLRLI NQGMVVLNGA KMSKSKGNIV EFSKEVSQHG VDVIRFALIF
     SGPPEEDIDW KDVSMTGAAR FLSRCIQTAK EVPKRTADLS LGDIELRKHT HSLLNDIDWL
     VDSYRFNVIA ARLMDLLNIT RKKIQTIGAD NPAIREAIET IAIALDMFSP YTAEEMWEIL
     GNKYSVSKAL FPEVDTTFLE QKTTCAIVQI DGRLRGRLNV LTNITTEQLV HSARSLPAIE
     HALSGRSVKR VICVPPKLVN FVVEPK
//