ID   SYL_STRPI               Reviewed;         833 AA.
AC   B1I8Y2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=SPH_0372;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
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; CP000936; ACA37591.1; -; Genomic_DNA.
DR   RefSeq; WP_000011744.1; NC_010380.1.
DR   AlphaFoldDB; B1I8Y2; -.
DR   SMR; B1I8Y2; -.
DR   EnsemblBacteria; ACA37591; ACA37591; SPH_0372.
DR   GeneID; 66805463; -.
DR   KEGG; spv:SPH_0372; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002163; 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; 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_1000091370"
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;  94384 MW;  07FABC51B8B69BA2 CRC64;
     MSFYNHKEIE PKWQGYWAEH HTFKTGTDAS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
     ILSRYKRAQG YNVLHPMGWD AFGLPAEQYA MDTGNDPAEF TAENIANFKR QINALGFSYD
     WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
     GYPVVRKPMR QWMLKITAYA ERLLNDLDEL DWPESIKDMQ RNWIGKSTGA NVTFKVKGTD
     KEFTVFTTRP DTLFGATFTV LAPEHELVDA ITSTEQAEAV ADYKHQASLK SDLARTDLAK
     EKTGVWTGAY AINPVNGKEI PIWIADYVLA SYGTGAVMAV PAHDQRDWEF AKQFDLPIVE
     VLEGGNVEEA AYTEDGLHVN SDFLDGLNKE DAIAKIVAWL EEKGCGQEKV TYRLRDWLFS
     RQRYWGEPIP IIHWEDGTST AVPESELPLV LPVTKDIRPS GTGESPLANL TDWLEVTRED
     GVKGRRETNT MPQWAGSSWY YLRYIDPHNT EKLADEDLLK QWLPVDIYVG GAEHAVLHLL
     YARFWHKFLY DLGVVPTKEP FQKLFNQGMI LGTSYRDHRG ALVATDKVEK RDGSFFHVET
     GEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
     LDRVYRLITS KEILAENNGA LDKVYNETVK AVTEQIESLK FNTAIAQLMV FVNAANKEDK
     LYVDYAKGFI QLIAPFAPHL AEELWQTVAE TGESISYVAW PTWDESKLVE DEIEIVVQIK
     GKVRAKLMVA KDLSREELQE IALADEKVKA EIDGKEIVKV IAVPNKLVNI VVK