ID   SYL_STAA8               Reviewed;         805 AA.
AC   Q2FXH2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 117.
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};
GN   OrderedLocusNames=SAOUHSC_01875;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; CP000253; ABD30940.1; -; Genomic_DNA.
DR   RefSeq; WP_001549041.1; NZ_LS483365.1.
DR   RefSeq; YP_500378.1; NC_007795.1.
DR   AlphaFoldDB; Q2FXH2; -.
DR   SMR; Q2FXH2; -.
DR   STRING; 93061.SAOUHSC_01875; -.
DR   BindingDB; Q2FXH2; -.
DR   ChEMBL; CHEMBL4295595; -.
DR   PaxDb; 1280-SAXN108_1789; -.
DR   GeneID; 3921764; -.
DR   KEGG; sao:SAOUHSC_01875; -.
DR   PATRIC; fig|93061.5.peg.1707; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..805
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009438"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           577..581
FT                   /note="'KMSKS' region"
FT   BINDING         580
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   805 AA;  91786 MW;  CCEF7840099E907F CRC64;
     MLNYNHNQIE KKWQDYWDEN KTFKTNDNLG QKKFYALDMF PYPSGAGLHV GHPEGYTATD
     IISRYKRMQG YNVLHPMGWD AFGLPAEQYA LDTGNDPREF TKKNIQTFKR QIKELGFSYD
     WDREVNTTDP EYYKWTQWIF IQLYNKGLAY VDEVAVNWCP ALGTVLSNEE VIDGVSERGG
     HPVYRKPMKQ WVLKITEYAD QLLADLDDLD WPESLKDMQR NWIGRSEGAK VSFDVDNTEG
     KVEVFTTRPD TIYGASFLVL SPEHALVNSI TTDEYKEKVK AYQTEASKKS DLERTDLAKD
     KSGVFTGAYA TNPLSGEKVQ IWIADYVLST YGTGAIMAVP AHDDRDYEFA KKFDLPIIEV
     IEGGNVEEAA YTGEGKHINS GELDGLENEA AITKAIQLLE QKGAGEKKVN YKLRDWLFSR
     QRYWGEPIPV IHWEDGTMTT VPEEELPLLL PETDEIKPSG TGESPLANID SFVNVVDEKT
     GMKGRRETNT MPQWAGSCWY YLRYIDPKNE NMLADPEKLK HWLPVDLYIG GVEHAVLHLL
     YARFWHKVLY DLAIVPTKEP FQKLFNQGMI LGEGNEKMSK SKGNVINPDD IVQSHGADTL
     RLYEMFMGPL DAAIAWSEKG LDGSRRFLDR VWRLMVNEDG TLSSKIVTTN NKSLDKVYNQ
     TVKKVTEDFE TLGFNTAISQ LMVFINECYK VDEVYKPYIE GFVKMLAPIA PHIGEELWSK
     LGHEESITYQ PWPTYDEALL VDDEVEIVVQ VNGKLRAKIK IAKDTSKEEM QEIALSNDNV
     KASIEGKDIM KVIAVPQKLV NIVAK
//