ID   SYL_BORBZ               Reviewed;         840 AA.
AC   B7J1H9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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};
GN   OrderedLocusNames=BbuZS7_0257;
OS   Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=445985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS7;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
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; CP001205; ACK75155.1; -; Genomic_DNA.
DR   RefSeq; WP_012597411.1; NC_011728.1.
DR   AlphaFoldDB; B7J1H9; -.
DR   SMR; B7J1H9; -.
DR   KEGG; bbz:BbuZS7_0257; -.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   Proteomes; UP000006901; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_1000199181"
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;  98217 MW;  521EA46AF0095A3D CRC64;
     MSKYEFIKIE KKWQEFWDNN KTYKVEEDPS IPKEKRLYIL DMFPYPSANG LHVGHPEGYT
     ATDIFGRYKL LNGFHVLHPI GFDSFGLPAE NYAIQTGTHP QKSTEENINK FKKQIKALGF
     AYDWDREIRT HEENYYKWTQ WIFLQLYKKG LAYVKEMPVW YCPELGTVLA NEEIIQTSDG
     PKSERGSYSV EKKYLRQWVL KITKYAERLL DDLEELEWPE SVKEMQRNWI GKSTGVEIEF
     EIEGHSDKIK VFTTRPDTIF GITYLVIAPE NKLIEKITKN NFKQNVLKYV KHEELKSDLN
     RTSLEKDKSG VFTGSYAFHP ITNEKIPIWV GSYVLGTYGT GAVMGVPAHD ERDFQFAKKY
     QLKILPVISK SGKNEILEKA FVDDGISINS PNEFNNLKNS EVKDKVIKWL TKNKKGKEKV
     AYKLRDWIFS RQRYWGEPIP ILFDKLGNAI PLEENDLPLK LPEIANYKPS GTGESPLSRI
     KDWVNVKDMG FTRETNTMPQ WAGSCWYYLR YLDPKNSKEF ANKKKIEYWM PVDLYIGGAE
     HTVLHLLYSR FWHKVLYDLG YVNTKEPFKK LINQGIITSF SYQKENGVLI PNDQVIEKDN
     KFFDKKDNKE VTQVIAKMSK SLKNVINPDD IIKEFGADSM RIYEMFMGPL TDSKPWNTKG
     IIGVFRFLNK IWNLREKELS KENPPREIIS ELHKVIKKVT EDTEKLNFNT AISAMMIFIN
     ELLKYEKNYL NIFKPFIIIL SPYAPHLAEE LWEYIGELPS LFKNSKWPKF DESLIIKDKK
     EIVLQINGKI KDKILLNKET GEKELKEIAM ENSKIKSNLL NKKIVKIIVI KNKLVNIVIK
//