ID   SYL_LISMH               Reviewed;         803 AA.
AC   B8DFR1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=LMHCC_0905;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(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; CP001175; ACK39254.1; -; Genomic_DNA.
DR   RefSeq; WP_012581211.1; NC_011660.1.
DR   AlphaFoldDB; B8DFR1; -.
DR   SMR; B8DFR1; -.
DR   KEGG; lmh:LMHCC_0905; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
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_1000199212"
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;  91882 MW;  35DE1629702BEF0A CRC64;
     MTFNHKKMEP KWQQYWSEHN TFKTTEDKNK ENFYALDMFP YPSGAGLHVG HPEGYTATDI
     LSRMKRMQGK NVLHPIGWDA FGLPAEQYAI DTGNDPEEFT ALNIANFTRQ IKSLGFSYDW
     DREINTTDPE YYKWTQWIFE KLYENGLAYE AEIAVNWCPA LGTVLANEEV IDGKSERGGF
     PVFRKPMRQW MLKITAYADR LLDDLDLVDW PENIKDMQRN WIGRSEGAEV TFKIKDSDET
     FNVFTTRPDT LFGATYTVFA PEHELIEKIT TPEQKEAVEA YKKQVELKSE LERTDLAKDK
     TGVFTGAYAI NPINGEEVPI WIADYVLIQY GTGAIMAVPA HDERDFEFAQ QFGLNIRPVL
     EGGDVTKEAF TGDGPHINSD FLNGLAKAEA ITAAIDWLEK EGIGSRKITY RLRDWLFSRQ
     RYWGEPIPVI HWEDGETTLV PEDELPLLLP KATEIKPSGT GESPLANLHD WVNVTDENGR
     KGRRETNTMP QWAGSSWYFL RYIDPKNSEA IADKEKLAEW LPVDVYIGGA EHAVLHLLYA
     RFWHKFLYDI GVVPTKEPFQ KLFNQGMILG ENNEKMSKSR GNVVNPDEVV EKYGADTLRL
     YEMFMGPLEA SIAWNENGLE GARKFLDRIW RLLVTEEGTL AEKVTTDANA NLEKAYHHMV
     KTVTNHYENL RFNTGISQLM IFINEAYKQD TIPKQYVEGF VQLLSPIAPH LAEELWEILG
     HTETISYVAW PTYDETKLVE DEVEIVLQVN GKVKSKITVA KSLGKEELEK IAQEDNKMKE
     NLEGKTIRKV IVVPGKLVNI VAN
//