ID   SYL_STRPZ               Reviewed;         833 AA.
AC   B5XJI9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Spy49_0152;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/jb.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(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; CP000829; ACI60501.1; -; Genomic_DNA.
DR   RefSeq; WP_012560407.1; NC_011375.1.
DR   AlphaFoldDB; B5XJI9; -.
DR   SMR; B5XJI9; -.
DR   EnsemblBacteria; ACI60501; ACI60501; Spy49_0152.
DR   KEGG; soz:Spy49_0152; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001039; 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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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_1000091372"
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;  93849 MW;  7CB57604CF75E133 CRC64;
     MTFYDHTAIE PKWQAFWADN HTFKTGTDAS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
     ILSRFKRAQG HNVLHPMGWD AFGLPAEQYA MDTGNDPAEF TAENIANFKR QINALGFSYD
     WDREVNTTDP NYYKWTQWIF TELYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
     GYPVVRKPMR QWMLKITAYA ERLLEDLEEV DWPESIKDMQ RNWIGKSTGA NVTFKVKDTD
     KDFTVFTTRP DTLFGATYAV LAPEHALVDA ITTADQAEAV ADYKRQASLK SDLARTDLAK
     EKTGVWTGSY AINPVNGNEM PVWIADYVLA SYGTGAIMAV PAHDERDWEF AKQFNLDIIP
     VLEGGNVEEA AFTEDGLHIN SDFLDGLDKA 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 PSYDKSKLVE NDVEIVVQIK
     GKVKAKLVVA KDLSREELQE VALANEKVQA EIAGKDIIKV IAVPNKLVNI VIK