ID   SYL_TREDE               Reviewed;         858 AA.
AC   Q73K81;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=TDE_2339;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12857.1; -; Genomic_DNA.
DR   RefSeq; NP_972938.1; NC_002967.9.
DR   RefSeq; WP_002680258.1; NC_002967.9.
DR   AlphaFoldDB; Q73K81; -.
DR   SMR; Q73K81; -.
DR   STRING; 243275.TDE_2339; -.
DR   EnsemblBacteria; AAS12857; AAS12857; TDE_2339.
DR   GeneID; 2739434; -.
DR   KEGG; tde:TDE_2339; -.
DR   PATRIC; fig|243275.7.peg.2207; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008212; 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; 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; 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; 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..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152108"
FT   MOTIF           43..54
FT                   /note="'HIGH' region"
FT   MOTIF           629..633
FT                   /note="'KMSKS' region"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   858 AA;  98404 MW;  087F7974B04C5837 CRC64;
     MAYPFSTIEP KWQKYWEENK TFKTVEDKNY PKDKRLYILD MFPYPSGDGL HVGHPEGYTA
     TDIYSRFLRM SGYNVLHPMG FDSFGLPAEN YAIKTGIHPL ITTRKNMETF RKQIKSIGLS
     YDWDREISTS EESYYKWTQW IFLQLFKKGL AYEKEAPINW CPSCLTGLAN EEVKDGKCER
     CGAQIQRKNL RQWILKITEY AERLLEDLDE LDWPESIKIM QKNWIGKSTG AEVDFALVDK
     DGKETGQKIK VYTTRPDTIF GATYMVLAPE HELVKSITTS NQEKAVAAYI EEAAKKSDLE
     RTDLAKNKTG VFTGAYAINP LTEQKIPVWI SDYILISYGT GAIMAVPAHD ERDFEFAAQF
     NLPKIKVVAG AEEWESGKRD FSEEPKACTT EDGYSVNSKQ FDGLKTEEAK TKITEHLENL
     GIAKRAVNYK LRDWIFSRQR YWGEPIPLVH CPSCGIVPLN EHDLPLTLPQ VESYAPTGTG
     ESPLAAIDSW VNTKCPKCGK EAKRETNTMP QWAGSCWYYL RFIDPHNNEA FADKEKCDYW
     MPVDLYVGGT EHAVLHLLYA RFWHKVLYDL GLVSTKEPFT RLINQGMITS FAYMRKNKSL
     VPVDKVKKIS ETEFEDIETG EKLEQVIAKM SKSLKNVINP DDIIKEYGAD TLRLYEMFLG
     PLEVSKPWNT SGIMGVFRFL EKIWNLSDRE IYKTPVNDTS TPETKTLTVL LNKTIKKVTE
     DTASLNFNTA ISQMMIFINE VSKHKKIPHY VWYNFVKLLN PYAPHLAEEL WQKMGNDESI
     AYSHWPMFVE KFCVDQTCTV VVQVNGKLRG KFEAEAGTSK EELERLALSN EGAIRNIEGK
     EIKKIITVPD KLVNIVVQ