ID   SYL_LACLA               Reviewed;         829 AA.
AC   Q9CHB6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=LL0816;
GN   ORFNames=L0352;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK04914.1; -; Genomic_DNA.
DR   PIR; H86726; H86726.
DR   RefSeq; NP_266972.1; NC_002662.1.
DR   RefSeq; WP_003132571.1; NC_002662.1.
DR   AlphaFoldDB; Q9CHB6; -.
DR   SMR; Q9CHB6; -.
DR   PaxDb; 272623-L0352; -.
DR   EnsemblBacteria; AAK04914; AAK04914; L0352.
DR   KEGG; lla:L0352; -.
DR   PATRIC; fig|272623.7.peg.872; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002196; 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; Reference proteome.
FT   CHAIN           1..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152029"
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;  93791 MW;  F0F0A43014F6C389 CRC64;
     MEYNHQEIEA 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
//