ID   SYL_THEMA               Reviewed;         824 AA.
AC   Q9WY15;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 143.
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=TM_0168;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD35261.1; -; Genomic_DNA.
DR   PIR; F72408; F72408.
DR   RefSeq; NP_227983.1; NC_000853.1.
DR   RefSeq; WP_004082796.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WY15; -.
DR   SMR; Q9WY15; -.
DR   STRING; 243274.THEMA_03960; -.
DR   EnsemblBacteria; AAD35261; AAD35261; TM_0168.
DR   KEGG; tma:TM0168; -.
DR   eggNOG; COG0495; Bacteria.
DR   InParanoid; Q9WY15; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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; 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   PANTHER; PTHR43740; PTHR43740; 2.
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; 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..824
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152106"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   824 AA;  95625 MW;  7CB0252A76A844EC CRC64;
     MKEYRPQEIE KKWQEVWEEK KVFYTPQRSE KPKYYALVMF PYPSGTLHVG HVKNYVIGDI
     VARYKRMRGY NVLHPFGYDA FGLPAENAAI EKGIHPEEWT RKNIATIRQQ VKKLGISYDW
     SREIATCDEE YYKWTQWIFL QLYKNGLAYK KKAAVNWCPK CKTVLANEQV KDGKCERCGT
     SVTIRHLEQW FFKITDYAER LLNDLDKLTG WPEHVKTMQR NWIGKSTGAE IDFPVEGSDT
     KIRVFTTRPD TLWGVTFMAL APESPLVEEL VPEEKKEELQ EFLERVKQQD RFRRTSVEAE
     KEGFFLGRYA INPVTGERIP IYVANYILME YGTGAIMGVP AHDQRDFSFA KKYGIPIKVV
     IKPADKDLDP EKMEEAYEGE GIMVNSGPFD GTPSSEGIEK VINWLEEKGI GKRSVQYKLR
     DWLISRQRYW GAPIPIIYCE KCGVVPVPEE DLPVRLPKDV EFLPTGQSPL SFHEGFKKTK
     CPVCGGEAQR ETDTMDTFVD SSWYFLRYVN PHLEDKPFEP DDVNYWLPVD QYIGGVEHAV
     LHLLYSRFVT KVLHDLGYLN FDEPFTNLFT QGMIYKDGAK MSKSKGNVVS PDEMIEKYGA
     DTLRMYILFM APPEKDAEWS DAGIEGVHRF VKRLWNTFYT VLPFVKEENT ENLVLKNSTE
     KELRRKLHSI IKKITEDIEG GFKFNTAISG LMELVNHLSQ YLNSVPQEEW NRKLLREIVE
     KLTLALSPFA PHLAEEFWHD LGNDSLVVQQ SWPSYDPKAL EVEEVEIAIQ INGKVRDKVV
     VPVDISEEDL KRIVLERERV KEYVDGKPIR KFIYVKGRIV NIVV