ID   SYL_STAAW               Reviewed;         807 AA.
AC   Q8NW17;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=MW1701;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95566.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NW17; -.
DR   SMR; Q8NW17; -.
DR   EnsemblBacteria; BAB95566; BAB95566; BAB95566.
DR   KEGG; sam:MW1701; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000418; 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   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; 2.
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..807
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152087"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           579..583
FT                   /note="'KMSKS' region"
FT   BINDING         582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   807 AA;  91984 MW;  0E1E28BB1695AEC4 CRC64;
     MLNYNHNQIE KKWQDYWDEN KTFKTNDNLG QKKFYALDMF PYPSGAGLHV GHPEGYTATD
     IISRYKRMQG YNVLHPMGWD AFGLPAEQYA LDTGNDPREF TKKNIQTFKR QIKELGFSYD
     WDREVNTTDP EYYKWTQWIF IQLYNKGLAY VDEVAVNWCP ALGTVLSNEE VIDGVSERGG
     HPVYRKPMKQ WVLKITEYAD QLLADLDDLD WPESLKDMQR NWIGRSEGAK VSFDVDNTEA
     EGKVEVFTTR PDTIYGASFL VLSPEHALVN SITTDEYKEK VKAYQTEASK KSDLERTDLA
     KDKSGVFTGA YAINPLSGEK VQIWIADYVL STYGTGAIMA VPAHDDRDYE FAKKFDLPII
     EVIEGGNVEE AAYTGEGKHI NSGELDGLEN EAAITKAIQL LEQKGAGEKK VNYKLRDWLF
     SRQRYWGEPI PVIHWEDGTM TTVPEEELPL LLPETDEIKP SGTGESPLAN IDSFVNVVDE
     KTGMKGRRET NTMPQWAGSC WYYLRYIDPK NENMLADPEK LKHWLPVDLY IGGVEHAVLH
     LLYARFWHKV LYDLGIVPTK EPFQKLFNQG MILGEGNEKM SKSKGNVINP DDIVQSHGAD
     TLRLYEMFMG PLDAAIAWSE KGLDGSRRFL DRVWRLMVNE DGTLSSKIVT TNNKSLDKVY
     NQTVKKVTED FETLGFNTAI SQLMVFINEC YKVDEVYKPY IEGFVKMLAP IAPHIGEELW
     SKLGHEESIT YQPWPTYDEA LLVDDEVEIV VQVNGKLRAK IKIAKDTSKE EMQEIALSND
     NVKASIEGKD IMKVIAVPQK LVNIVAK