ID   SYL_BORHD               Reviewed;         842 AA.
AC   B2RZW1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BH0251;
OS   Borrelia hermsii (strain HS1 / DAH).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 / DAH;
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; CP000048; AAX16767.1; -; Genomic_DNA.
DR   RefSeq; WP_012422024.1; NC_010673.1.
DR   AlphaFoldDB; B2RZW1; -.
DR   SMR; B2RZW1; -.
DR   KEGG; bhr:BH0251; -.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
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_1000091293"
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;  98521 MW;  6826EF84209307EA CRC64;
     MSEYNFTKIE KKWQDYWDKH KTYKVNEDPN IPKEKRIYIL DMFPYPSANG LHVGHPEGYT
     ATDILTRYKL LNGFNVLHPI GFDSFGLPAE NYAIQTGEHP KKITEKNIKK FKEQIKALGF
     AYDWDREIRT HDENYYKWTQ WIFLKLYKKG LAYTKEMPVW YCPDLGTVLS NEEVIQTPDG
     PRSERGFHKV KRKPLRQWIL KITEYAERLI KDLEEIDWPE SVKEMQKNWI GKSTGAEIEF
     SVKASKEKIK VFTTRPDTIF GVTYLVLAPE HSIVDKITKD EFKPMIVEYR ERETLKSDLE
     RTSLEKDKTG VFTGAYAINP ITGEEIPIWI GSYILGTYGT GAVMSVPAHD ARDFEFAKKY
     NLPIKQVVSQ TGNNEILTQP FTENGISINT PEEFNNLKTD EIKERVIKWL TENKKGQKKV
     NYKLRDWIFS RQRYWGEPIP IILDDDLNEI PLEEDELPLR LPEIENYKPS GTGESPLSRI
     QDWVNIKRNG KTYKRETNTM PQWAGSCWYY IRYLDPNNDN EFASKEKINY WMPVDLYIGG
     AEHSVLHLLY ARFWHKVLYD LGYVNTKEPF KKLINQGMIT SFAYQDENGI LIPNDEVEKK
     DNKFFSKKNN KELKQIVAKM SKSLKNIINP DDIIKEYGAD SMRIYEMFMG PLTDSKPWNT
     QGLIGIFRFL NKIWTIKNKE LTKESASKEI ISELHKTIKK VTEDIENLNF NTAISSLMIF
     INELLKHDKN YLEIFKPLTI ILSPFAPHLG EELWEYMGET PSIFKSAKWP EYDPNLIIDN
     TREIVLQING KIKDKIILNK GTNEEALKSI ALKNHKIMQN IQNKQIIKII TVKDKLINIV
     TR