ID   SYL_BORRA               Reviewed;         842 AA.
AC   B5RR67;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BRE_252;
OS   Borrelia recurrentis (strain A1).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000993; ACH94501.1; -; Genomic_DNA.
DR   RefSeq; WP_012538770.1; NC_011244.1.
DR   AlphaFoldDB; B5RR67; -.
DR   SMR; B5RR67; -.
DR   EnsemblBacteria; ACH94501; ACH94501; BRE_252.
DR   KEGG; bre:BRE_252; -.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000612; 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_1000091294"
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;  98708 MW;  1636331275CE01F9 CRC64;
     MSKYDFKKIE KKWQNYWDKH KTYKVNEDPN VPKEKRIYIL DMFPYPSANG LHVGHPEGYT
     ATDILTRYKL LNGFNVLHPM GFDSFGLPAE NYAIQTGKHP KKITEKNIEK FKEQIKALGF
     AYDWDREIKT HDVNYYKWTQ WIFLQLYKKG LAYTKEIPVW YCPDLGTVLA NEEVIQTPDG
     PRSERGFHKV ERKPLRQWLL KITKYAERLI RDLEEVDWPD SVKEMQKNWI GKSTGVEIEF
     LIKESKEKIK VFTTRPDTIF GVTYLVLAPE HPMVDKITKD ELKPIISKYK DKEILKSDLE
     RTSLEKDKTG IFTGAYAINP ITKEEIPIWI GSYILGTYGT GAVMSVPAHD ERDFEFAKKY
     NLPIKQVVSQ TGTNEVLIKP FTENGISINT PTEFNNLKTI EVKTKVIKWL IENKMGQEKV
     NYKLRDWIFS RQRYWGEPIP ILFDDNLNEI PLNDDELPLT LPDIENYKPS GTGESPLSKI
     KDWVNVKRNG KIYKRETNTM PQWAGSCWYY IRYLDPHNEK EFANKEKINY WMPVDLYIGG
     AEHSVLHLLY ARFWHKVLYD LGYVNIKEPF RKLINQGMIT SFAYQDENGI LIPNDEVEKK
     DNKFFSKKNN KELKQIIAKM SKSLKNIINP DDIIKEYGAD SMRIYEMFMG PLTDSKPWNT
     QGLIGIFRFL NKIWLIKNKE LTNETPPKEI ISELHKTIKK VTEDIETLNF NTAISTLMIF
     INELLKHEKN YLKIFRPISI ILSPFAPHLG EELWEFMGEQ SSIFKNAKWP KYDLNSIIDD
     TREIVLQVNG KTKDKIMIKK DTDEKTLKKI AFNNQKIIQN INNKQIIKII TVKDKLVNIV
     AK