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 27-MAR-2024, entry version 91.
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; Pseudomonadota; 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 KEGG; btr:BT_2478; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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; 2.
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..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
//
