ID   SYL_STRPQ               Reviewed;         833 AA.
AC   P0DG45; Q8K8S1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=SPs0137;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
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; BA000034; BAC63232.1; -; Genomic_DNA.
DR   RefSeq; WP_011054143.1; NC_004606.1.
DR   AlphaFoldDB; P0DG45; -.
DR   SMR; P0DG45; -.
DR   KEGG; sps:SPs0137; -.
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; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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..833
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000411612"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           610..614
FT                   /note="'KMSKS' region"
FT   BINDING         613
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   833 AA;  93814 MW;  94A49BF43B2A1314 CRC64;
     MTFYDHTAIE PKWQAFWADN HTFKTGTDAS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
     ILSRFKRAQG HNVLHPMGWD AFGLPAEQYA MDTGNDPAEF TAENIANFKR QINALGFSYD
     WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
     GYPVVRKPMR QWMLKITVYA ERLLEDLEEV DWPESIKDMQ RNWIGKSTGA NVTFKVKDTD
     KNFTVFTTRP DTLFGATYAV LAPEHALVDA ITTADQAEAV ADYKRQASLK SDLARTDLAK
     EKTGVWTGSY AINPVNGKEI PVWIADYVLA SYGTGAIMAV PAHDERDWEF AKQFNLDIIP
     VLEGGNVEEA AFTEDGLHIN SGFLDGLDKA SAIAKMVEWL EAEGVGNEKV TYRLRDWLFS
     RQRYWGEPIP IIHWEDGTST AVPESELPLV LPVTKDIRPS GTGESPLANV TDWLEVTRED
     GVKGRRETNT MPQWAGSSWY YLRYIDPHNT EKLADEELLK QWLPVDIYVG GAEHAVLHLL
     YARFWHKVLY DLGVVPTKEP FQKLFNQGMI LGTSYRDSRG ALVATDKVEK RDGSFFHVET
     GEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
     LDRVYRLITT KEITEENSGA LDKVYNETVK AVTEQVDQMK FNTAIAQLMV FVNAANKEDK
     LFSDYAKGFV QLIAPFAPHL GEELWQALTA SGESISYVPW PSYDESKLVE NDVEIVVQIK
     GKVKAKLVVA KDLSREELQE VALANEKVQA EIAGKDIIKV IAVPNKLVNI VIK
//