ID   SYL_LIGS1               Reviewed;         805 AA.
AC   Q1WUT3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=LSL_0442;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99252.1; -; Genomic_DNA.
DR   RefSeq; WP_011475758.1; NC_007929.1.
DR   RefSeq; YP_535335.1; NC_007929.1.
DR   AlphaFoldDB; Q1WUT3; -.
DR   SMR; Q1WUT3; -.
DR   STRING; 362948.LSL_0442; -.
DR   GeneID; 69723703; -.
DR   KEGG; lsl:LSL_0442; -.
DR   PATRIC; fig|362948.14.peg.518; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006559; 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; 3.10.20.590; -; 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; Reference proteome.
FT   CHAIN           1..805
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009361"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   805 AA;  92215 MW;  255216A43873B93C CRC64;
     MSYKHIEIEK KWQRYWEEHK TFKTTEDDDK KNYYALDMFP YPSGQGLHVG HPEGYTATDI
     MARMKRMQGY NVLHPMGWDA FGLPAEQYAL NTGNSPREFT KKNVNNFRRQ IKSLGLSYDW
     DREVNTTDPA YYKWTQWIFE QLYKKGLAYE AEVPVNWSPD LGTVVANEEV IDGKTERGGF
     PVIRKPMRQW VLKITAYADR LIDDLDDLDW PEAIKEQQRN WIGRSVGAAI NFPVSGDENT
     KIEVFSTRPD TIFGVAALVL APEHELVKQL TTPEHENEVE AYIEKISHKS DLERTDLAKD
     KTGVFTGSYV VNPVSGEKLP IWIADYVLNS YGTGAVMVVP AHDERDHEFA QKFDLPIVQV
     IEGGDVQKEA YTGDGVHINS DFLNGMDKEE AIDAINNWLE ENGVGEKKVN YRLRDWLFSR
     QRYWGEPIPV IHWEDGETTL VPEDELPLYL PKATDIKPSG TGESPLANLD DWVNVVDENG
     RKGRRETNTM PQWAGSSWYF LRYIDPHNNH EIADYEKLKE WLPVNLYVGG AEHAVLHLLY
     ARFWHKFLYD LGVVPTKEPF QKLVNQGMIL GSNHEKMSKS KGNVVNPDDI VEQYGADTLR
     LYEMFMGPLD ASIPWSEEGL GGAHKFINRV WNLLIDENDN LRDRVTTINN HDLDKIYNET
     VKKVTEDYEA MHFNTAISQL MVFVNNAYKA DSLPLEYVEG LVKLLSPVVP HITEELWSKL
     GHVGSIAYAK WPTYDESKLV EDVVEIVVQI NGKVRQHLQV SKDASREELQ ALALNDERIK
     QELADKEVKK VIAVPGKLVS IVVAK
//