ID   SYL_STAAB               Reviewed;         804 AA.
AC   Q2YTH9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=SAB1618c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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}.
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DR   EMBL; AJ938182; CAI81307.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YTH9; -.
DR   SMR; Q2YTH9; -.
DR   KEGG; sab:SAB1618c; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
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   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.
FT   CHAIN           1..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009439"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  91655 MW;  DD957BB01CC274B3 CRC64;
     MNYNHNQIEK KWQDYWDENK TFKTNDNLGQ KKFYALDMFP YPSGAGLHVG HPEGYTATDI
     ISRYKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPREFT KKNIQTFKRQ IKELGFSYDW
     DREVNTTDPE YYKWTQWIFI QLYNKGLAYV DEVAVNWCPA LGTVLSNEEV IDGVSERGGH
     PVYRKPMKQW VLKITEYADQ LLADLDDLDW PESLKDMQRN WIGRSEGAKV SFDVDNTEGK
     VEVFTTRPDT IYGASFLVLS PEHALVNSIT TDEYKEKVKA YQTEASKKSD LERTDLAKDK
     SGVFTGAYAI NPLSGEKVQI WIADYVLSTY GTGAIMAVPA HDDRDYEFAK KFDLLIIEVI
     EGGNVEEAAY TGEGKHINSG ELDGLENEAA ITKAIQLLEQ KGAGEKKVNY KLRDWLFSRQ
     RYWGEPIPVI HWEDGTMTTV PEEELPLLLP ETDEIKPSGT GESPLANIDS FVNVVDEKTG
     MKGRRETNTM PQWAGSCWYY LRYIDPKNEN MLADPEKLKH WLPVDLYIGG VEHAVLHLLY
     ARFWHKVLYD LGIVPTKEPF QKLFNQGMIL GEGNEKMSKS KGNVINPDDI VQSHGADTLR
     LYEMFMGPLD AAIAWSEKGL DGSRRFLDRV WRLIVNEDGT LSSKIVTTNN KSLDKVYNQT
     VKKVTDDFET LGFNTAISQL MVFINECYKV DEVYKPYIEG FVKMLAPIAP HIGEELWSKL
     GHEESITYQP WPTYDEALLV DDEVEIVVQV NGKLRAKIKI AKDTSKEEMQ EIALSNDNVK
     ASIEGKDIMK VIAVPQKLVN IVAK
//