ID   SYL_LACLM               Reviewed;         829 AA.
AC   A2RLY6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=llmg_1741;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(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; AM406671; CAL98313.1; -; Genomic_DNA.
DR   RefSeq; WP_011835529.1; NZ_WJVF01000003.1.
DR   AlphaFoldDB; A2RLY6; -.
DR   SMR; A2RLY6; -.
DR   STRING; 416870.llmg_1741; -.
DR   KEGG; llm:llmg_1741; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; A2RLY6; -.
DR   Proteomes; UP000000364; 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; 3.40.50.620; 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; 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..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009359"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           609..613
FT                   /note="'KMSKS' region"
FT   BINDING         612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   829 AA;  93790 MW;  1502EA4E0E0BF67F CRC64;
     MEYNHQKIEA KWQKYWADNK TFRTGTDKNK PKFYALDMFP YPSGAGLHVG HPEGYTATDI
     LSRYKRAQGF NVLHPMGWDA FGLPAEQYAM DTGNDPAEFT AENIANFKRQ INSLGFSYDW
     EREVNTTDPN FYKWTQWIFT KLYEKGLAYE AEVAVNWVEE LGTAIANEEV LPDGTSERGG
     YPVVRKPMRQ WMLKITAYAE RLLEDLEEVD WPESIKEMQR NWIGKSVGAD VTFEVAGTDK
     SFEVFTTRPD TLFGATYAVL APEHDLVDAI TTPEQKEAVA EYRRKASLKS DLARTDLSKE
     KTGAFTGAYA INPINGRKMP IWVADYVLAS YGHGAVMAVP AHDERDWEFA KVYGLEILPV
     VEGGNVEEAV YTEDGPHINS EFLNGLDKAQ AIEKAIEFLE EKKIGKKKIT YRLRDWLFSR
     QRYWGEPIPI IHWEDGTSTA LSEDELPLVL PVTSDIKPSG TGESPLANLT DWLEVTRADG
     LKGRRETNTM PQWAGSSWYY LRYIDPNNSE ALADPELLKE WLPVDIYVGG AEHAVLHLLY
     ARFWHKVLYD LGVVPTKEPF QKLFNQGMIL GTSYRDHRGA LVATDKVEKR DGGFYHMETG
     EALEQAPAKM SKSLKNVVNP DDVVEHYGAD TLRVYEMFMG PLDASIPWSE EGLEGARKFL
     DRAVRMIENS EIKAENNGEL DKVYNETVKN VTERLDLMYF NTAISQLMIF VNAVNKAKAL
     PLEYANGFVQ LLAPFAPHIA EELWVKLGNE AGISYVAWPT FDESKLIESE VEIVVQINGK
     LKAKIKIAKD LAREELEKIG RESVAEALEG KNVVKVIAVP NKLVNIVVK
//