ID   SYL_STRZT               Reviewed;         833 AA.
AC   C1CPD0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, 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=SPT_0302;
OS   Streptococcus pneumoniae (strain Taiwan19F-14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Taiwan19F-14;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000921; ACO22249.1; -; Genomic_DNA.
DR   RefSeq; WP_000011770.1; NC_012469.1.
DR   AlphaFoldDB; C1CPD0; -.
DR   SMR; C1CPD0; -.
DR   KEGG; snt:SPT_0302; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
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; 1.
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_1000199229"
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;  94429 MW;  266435380B4EB01C CRC64;
     MSFYNHKEIE PKWQGYWAEH HTFKTGTDAS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
     ILSRYKRAQG YNVLHPMGWD AFGLPAEQYA MDTGNDPAEF TAENIANFKR QINALGFSYD
     WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
     GYPVVRKPMR QWMLKITAYA ERLLNDLDEL DWSESIKDMQ RNWIGKSTGA NVTFKVKGTD
     KEFTVFTTRP DTLFGATFTV LAPEHELVDA ITSSEQAEAV ADYKHQASLK SDLVRTDLAK
     EKTGVWTGAY AINPVNGKEM PIWIADYVLA SYGTGAVMAV PAHDQRDWEF AKQFDLPIVE
     VLEGGNVEEA AYTEDGLHVN SDFLDGLNKE DAIAKIVAYL EEKGCGQEKV TYRLRDWLFS
     RQRYWGEPIP IIHWEDGTST AVPETELPLV LPVTKDIRPS GTGESPLANL TDWLEVTRED
     GVKGRRETNT MPQWAGSSWY YLRYIDPHNT EKLADEDLLK QWLPVDIYVG GAEHAVLHLL
     YARFWHKFLY DLGVVPTKEP FQKLFNQGMI LGTSYRDHRG ALVTTDKVEK RDGSFFHVET
     GEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
     LDRVYRLITS KEILAENNGA LDKAYNETVK AVTEQIESLK FNTAIAQLMV FVNAANKEDK
     LYIDYAKGFI QLIAPFAPHL AEELWQTVAE TGESISYVAW PTWDESKLVE DEIEIVVQIK
     GKVRAKLMVA KDLSREELQE IALADEKVKA EIDGKEIVKV ISVPNKLVNI VVK