ID   SYL_BART1               Reviewed;         886 AA.
AC   A9IYY8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=BT_2478;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK02453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IYY8; -.
DR   SMR; A9IYY8; -.
DR   STRING; 382640.BT_2478; -.
DR   EnsemblBacteria; CAK02453; CAK02453; BT_2478.
DR   KEGG; btr:BT_2478; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001592; 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   Gene3D; 3.90.740.10; -; 1.
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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..886
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334731"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   886 AA;  100111 MW;  2065F8563BD3CE81 CRC64;
     MGMTIEHYKI GERYNPRARE KKWQEIWDEK KIFQTVQGDG REKYYVLEMF PYPSGRIHMG
     HVRNYAMGDV VARYKRAKGF NVLHPMGWDA FGMPAENAAL QSKVHPKTWT YENIAVMRGQ
     LKQLGLSLDW AREFATCDVD YYHRQQMLFL DFYQKGLVAR KVAKVNWDPV DHTVLANEQV
     VDGRGWRSGA LVEQRELTQW FFKISDFSED LLAGLEELDQ WPEKVRTMQK NWIGKSQGLL
     IRWALKSTAD DAGGSNDVCE AFDEVVCYST RPDTLFGASF LALSVDHPIA QSLAKKDKAL
     AAFIENCRCG GTTTAALETA EKQGFLTPLV AVHPFDETVH IPVYIANFVL MDYGTGAIFG
     CPAHDQRDFD FARKYDLPIK PVVLPRETKV EDFVLAEMPY TGDGVMINSS FLDGLTPQQA
     FEEVAKRLEQ QVLHGQPQGK KTVQFRLRDW GISRQRYWGC PIPMIHCTSC GVVPVPRADL
     PVVLPDDVTF DQPGNPLARH EMWQDVACPI CGQPAKRETD TMDTFVDSSW YYARFTAPFA
     PEPVEKQATA EWLPVQQYIG GIEHAILHLL YARFFMRAMK LVGHVSVDEP FKGLFTQGMV
     VHETYRDDQG WVSPAEISIV EKDGKRCAYK LTDQSEVTIG LIEKMSKSKK NVVDPDDIIA
     SYGADTVRWF VLSDSPPERD VIWTESGVEG AHRFVQRVWR HVALSAAVLK DVAPRAGHQG
     AALELSKAAH RMLHAVEDDL EKFAFNRAIA RLYEFLNIMA PLLNKVADVE DEMKAALRQA
     MDFFLAMIAP IMPHLAEECH AALGETTLMS ELAWPVYDPA LIVEESYTLP VQINGKKRGE
     VTVAATASET MIKEAVLALD FVQAQLVEKP MKKIIIVPQR IVNVVL