ID   SYL_BORT9               Reviewed;         842 AA.
AC   A1QZ46;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BT0251;
OS   Borrelia turicatae (strain 91E135).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91E135;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) 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; CP000049; AAX17588.1; -; Genomic_DNA.
DR   RefSeq; WP_011772207.1; NC_008710.1.
DR   AlphaFoldDB; A1QZ46; -.
DR   SMR; A1QZ46; -.
DR   STRING; 314724.BT0251; -.
DR   KEGG; btu:BT0251; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001205; 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; 2.
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.
FT   CHAIN           1..842
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199182"
FT   MOTIF           44..55
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   842 AA;  98516 MW;  9F82A1025E31B5A3 CRC64;
     MSEYNFTKIE KKWQNYWDKH KTYKVNEDPN IPKEKRIYIL DMFPYPSANG LHVGHPEGYT
     ATDILTRYKL LNGFNVLHPM GFDSFGLPAE NYAIQTGEHP KKITEKNIEK FKEQIKALGF
     AYDWDREIRT HDENYYKWTQ WIFLKLYKKG LAYIKEMPVW YCPDLGTVLS NEEVIQTPDG
     PRSERGFHKV QRKPLRQWVL KITEYAERLI KDLEEIDWPE SVKEMQKNWI GKSIGAEIEF
     SIKASKEKIK VFTTRPDTIF GVTYLVLAPE HNIVDKITKD ELKTIIAEYK DKEILKSDLE
     RTSLEKDKTG VFTGAYAINP ITEEEIPIWI GSYVLGIYGT GAVMSVPAHD ERDFEFAKKY
     NLPIKQVVSQ TGNNEILTKP FTENGISINT PEEFNNLKTE KVKTKVIEWL TKNKKGQKKV
     NYKLRDWIFS RQRYWGEPIP IIIDDDLNEI PLEEDELPLR LPEIENYKPS DTGESPLSKV
     QNWVNVKRNG KIYKRETNTM PQWAGSCWYY IRYLDPNNEK EFASKEKINY WMPVDLYIGG
     AEHSVLHLLY ARFWHKVLYD LGYVNTKEPF KKLINQGMIT SFAYQDENGI LIPNDEVKKR
     DNKFFSKTNN KELKQIIAKM SKSLKNIINP DDIIKEYGAD SMRIYEMFMG PLTDSKPWNT
     QGLIGIFRFL NKIWAIKNKE LTKESAAKEI ISGLHKTIKK VTEDIENLNF NTAISSLMIF
     INELLKHDKN YLEIFKPLTI ILAPFAPHLG EELWEYMGEQ PSIFKNAKWP KYDPNLIIDN
     TREIVLQVNG KIKDKIILNK GINEDTLKDI ALKNHKIMQN IQNKQIIKII TVKDKLINIV
     TK