ID   SYL_STRSY               Reviewed;         833 AA.
AC   A4VY58;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 90.
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=SSU05_2081;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP91047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000407; ABP91047.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A4VY58; -.
DR   SMR; A4VY58; -.
DR   STRING; 391295.SSU05_2081; -.
DR   PRIDE; A4VY58; -.
DR   EnsemblBacteria; ABP91047; ABP91047; SSU05_2081.
DR   KEGG; ssu:SSU05_2081; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   Proteomes; UP000000243; 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; Reference proteome.
FT   CHAIN           1..833
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334826"
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;  94010 MW;  60E45A43158ED41B CRC64;
     MSFYNHKEIE PKWQEFWAKN HTFKTGTDAE KPNFYALDMF PYPSGAGLHV GHPEGYTATD
     ILSRYKRAQG YNVLHPMGWD AFGLPAEQYA MDTGNDPADF TAENIANFKR QINALGFSYD
     WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
     GYPVVRKPMR QWMLKITAYA ERLLNDLEEV DWPESIKDMQ RNWIGKSTGA NVTFKIKDTD
     KDFTVFTTRP DTLFGATYAV LAPEHDLVDS ITSAEQAEAV AEYKRQASLK SDLARTDLAT
     DKTGVWTGAY AINPVNGKEI PIWIADYVLA SYGTGAIMAV PAHDERDWEF AKQFGLDIIP
     VLEGGNVEEA PYTEDGAHIN SDFLDGLNKE EAIAKMVAWL EENGVGQEKI SYRLRDWLFS
     RQRYWGEPIP IIHWEDGTST AVPENELPLV LPKTSDIKPS GTGESPLANL TDWLEVVRED
     GVKGRRETNT MPQWAGSSWY YLRYIDPHND EKLADEDLLK AWLPVDIYIG GAEHAVLHLL
     YARFWHKFLY DLGVVPTKEP FQKLFNQGMI LGTSYRDSRG ALVATDKVEK RDGSFFHMET
     GEELEQAPAK MSKSLKNVVN PDDVVEQFGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
     LDRVYRLLTT KELVAENSGA LDKVYNETVK TVTEHIEDLK FNTAIAQLMI FVNAANKEDK
     LYVDYAKGFV QLIAPFAPHL AEELWQGLAN TGQSISYVAW PTYDESKLVE SEVEIVVQIK
     GKVKARLTVA KDLAPAELEK VALADEKVQA EIAGQTVVKV ISVPNKLVNI VVK