ID   SYL_LEUCK               Reviewed;         803 AA.
AC   B1MY11;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=LCK_00580;
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20;
RX   PubMed=18281406; DOI=10.1128/jb.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82413.1; -; Genomic_DNA.
DR   RefSeq; WP_004908127.1; NC_010471.1.
DR   AlphaFoldDB; B1MY11; -.
DR   SMR; B1MY11; -.
DR   STRING; 349519.LCK_00580; -.
DR   GeneID; 61102488; -.
DR   KEGG; lci:LCK_00580; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002166; 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.
FT   CHAIN           1..803
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091334"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           575..579
FT                   /note="'KMSKS' region"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   803 AA;  91586 MW;  2E4AF1E47D8BE59C CRC64;
     MPYEHQQIEQ KWQKFWDDNQ TFATSDTTDK PKYYAVDMFP YPSGQGLHVG HPEGYTATDI
     MSRFKRAKGF NVLHPMGWDA FGLPAEQYAM KTGHNPADFT SQNIDHFREQ IKSLGLSYDW
     NREINTTDPS YYKWTQWIFE KLYEKGLAYE SNMMVNWDPI DRVVLANEEV IDGKSERSGN
     KVERKALRQW VLKITAYADR LVDDLDDLDW PEAIKEQQRN WIGRSKGAAV FFNVDHADAK
     IEVYTTRPDT LFGATYMVLA PEHELVDSIV TAEQKQAVAD YRAAIAAKSD LERTDLNKDK
     TGVFTGAYGI NPINGEKLPI WIADYVLASY GTGAIMAVPA HDDRDFEFAK KFDLAIKPVI
     AGGENDDVAY TGDGVHINSD FLDGLDKATA IDQAIDWLEA HQAGHAQTNF RLRDWIFSRQ
     RYWGEPIPVI HWEDGTTSLV PENELPLLLP HATELRPSGS GESPLANLTD WLEVTRDDGV
     KGRRETNTMP QWAGSSWYFL RYIDPHNDHQ LADPEKLKYW MNVDLYVGGA EHAVLHLLYA
     RFWHKFLYDL GVVPTKEPFQ KLVNQGMILG ANHEKMSKSK GNVVNPDDIV REYGADTLRV
     YEMFMGPLTQ SKPWSEEGIT GSRRWLDRVW RLLIDDEGQL RDHVTTVNPG DLDKIYHQTV
     KKVTDDLENM RFNTAISQMM VFVNDAYKSD ALPVTYMNGF IQLLAPFAPH LAEELWVRLG
     NRESISYVSW PTYDDTKLVD DTVEIIFQVN GKVRGKATVA RDINQDDMIT AAKADDNVQN
     FITGKTVRKV IAIPGKFVNI VVS
//