ID   SYL_BORGP               Reviewed;         840 AA.
AC   Q662B4;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=BG0254;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(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; CP000013; AAU07107.1; -; Genomic_DNA.
DR   RefSeq; WP_011193591.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q662B4; -.
DR   SMR; Q662B4; -.
DR   STRING; 290434.BG0254; -.
DR   EnsemblBacteria; AAU07107; AAU07107; BG0254.
DR   KEGG; bga:BG0254; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002276; 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..840
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151980"
FT   MOTIF           44..55
FT                   /note="'HIGH' region"
FT   MOTIF           617..621
FT                   /note="'KMSKS' region"
FT   BINDING         620
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   840 AA;  98168 MW;  20A9FBE916589685 CRC64;
     MSKYEFIKIE KKWQEFWDNN KTYKVKEDPN IPKEKRLYIL DMFPYPSANG LHVGHPEGYT
     ATDIFGRYKL LNGFHVLHPI GFDSFGLPAE NYAIQTGTHP QKSTEENINK FKKQIKALGF
     AYDWDREIRT HDENYYKWTQ WIFLELYKKG LAYAKEMPVW YCPELGTVLA NEEIIQTPDG
     PKSERGFHNV EKKYLRQWVL KITKYAERLL NDLEELEWPE SVKEMQRNWI GKSTGVEIDF
     EIEGHNDKIK VFTTRPDTIF GITYLVIAPE SKLIEKITKN NFKRNVLKYV KHEELKSDLK
     RTSLEKDKSG VFTGSYAFHP ITNEKIPIWI GSYVLGTYGS GAVMGVPAHD ERDFQFAKKY
     KLKILPVISK SGKNEILEKA FIDDGISINS PNEFNNLKNS EVKDKVIEWL IKNKKGKEKV
     TYKLRDWIFS RQRYWGEPIP ILFDKLGNAV PLEKNDLPLK LPKTANYKPS RTGESPLSRI
     KDWVNLKDTG FTRETNTMPQ WAGSCWYYLR YLDPKNPKEF ASKKKIEYWM PVDLYIGGAE
     HTVLHLLYSR FWHKVLYDLG YVNTKEPFKK LINQGIITAF SYQKENGILI PNDQVIEKNS
     KFFDKRDNKE VIQVIAKMSK SLKNVINPDD IIKEFGADSI RIYEMFMGPL TDSKPWNTKG
     IIGVFRFLNK IWNLREKELS KDNPPKEIIS QLHKAIKKVT EDTEKLSFNT AISAMMIFVN
     ELIKYEKNYL NIFKPFIIIL SPYAPHLAEE LWEYIGETPS LFKNSKWPEF DENLIIKDAK
     EIVLQINGKM KDKILLSKET DEEELKEIAM GNSKIKANLL NKKIVKIIAI KNKLVNIVIK