ID   SYL_STAAS               Reviewed;         806 AA.
AC   Q6G8G9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SAS1684;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43487.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6G8G9; -.
DR   SMR; Q6G8G9; -.
DR   KEGG; sas:SAS1684; -.
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   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..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152086"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           578..582
FT                   /note="'KMSKS' region"
FT   BINDING         581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  91871 MW;  6063BAAE9233B62B CRC64;
     MNYNHNQIEK KWQDYWDENK TFKTNDNLGQ KKFYALDMFP YPSGAGLHVG HPEGYTATDI
     ISRYKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPREFT KKNIQTFKRQ IKELGFSYDW
     DREVNTTDPE YYKWTQWIFI QLYNKGLAYV DEVAVNWCPA LGTVLSNEEV IDGVSERGGH
     PVYRKPMKQW VLKITEYADQ LLADLDDLDW PESLKDMQRN WIGRSEGAKV SFDVDNTEAE
     GKVEVFTTRP DTIYGASFLV LSPEHALVNS ITTDEYKEKV KAYQTEASKK SDLERTDLAK
     DKSGVFTGAY AINPLSGEKV QIWIADYVLS TYGTGAIMAV PAHDDRDYEF AKKFDLPIIE
     VIEGGNVEEA AYTGEGKHIN SGELDGLENE AAITKAIQLL EQKGAGEKKV NYKLRDWLFS
     RQRYWGEPIP VIHWEDGTMT TVPEEELPLL LPETDEIKPS GTGESPLANI DSFVNVVDEK
     TGMKGRRETN TMPQWAGSCW YYLRYIDPKN ENMLADPEKL KHWLPVDLYI GGVEHAVLHL
     LYARFWHKVL YDLGIVPTKE PFQKLFNQGM ILGEGNEKMS KSKGNVINPD DIVQSHGADT
     LRLYEMFMGP LDAAIAWSEK GLDGSRRFLD RVWRLMVNED GTLSSKIVTT NNKSLDKVYN
     QTVKKVTEDF ETLGFNTAIS QLMVFINECY KVDEVYKPYI EGFVKMLAPI APHIGEELWS
     KLGHEESITY QPWPTYDEAL LVDDEVEIVV QVNGKLRAKI KIAKDTSKEE MQEIALSNDN
     VKASIEGKDI MKVIAVPQKL VNIVAK