ID   SYL_STAES               Reviewed;         804 AA.
AC   Q8CNU8;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 124.
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=SE_1431;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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=AAO05030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE015929; AAO05030.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_764986.1; NC_004461.1.
DR   RefSeq; WP_002493961.1; NZ_WBME01000009.1.
DR   AlphaFoldDB; Q8CNU8; -.
DR   SMR; Q8CNU8; -.
DR   STRING; 176280.SE_1431; -.
DR   EnsemblBacteria; AAO05030; AAO05030; SE_1431.
DR   GeneID; 50018459; -.
DR   KEGG; sep:SE_1431; -.
DR   PATRIC; fig|176280.10.peg.1397; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   Proteomes; UP000001411; 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..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152088"
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;  92164 MW;  173B55466D9C0725 CRC64;
     MNYNHKEIEK KWQNYWEENK TFKTNDNLGQ KKFYALDMFP YPSGAGLHVG HPEGYTATDI
     ISRYKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPREFT QKNIQTFKRQ IQELGFSYDW
     DREVNTTDPE YYKWTQWIFI QLYNKGLAYV DEVAVNWCPA LGTVLSNEEV VDGVSERGGH
     PVYRKPMKQW VLKITEYADR LLEDLDELDW PESIKDMQRN WIGRSEGAKV TFKIEQSDQN
     IEVFTTRPDT IYGTSFLVLS PEHPLVNEIT TSDKEQEVKL YQNEASKKSD LERTDLAKEK
     TGVFTGTFAI NPLSGDKLPI WIADYVLSTY GTGAVMAVPG HDERDHEFAT KFNLPIIEVI
     EGGEVQKYAY TGEGKHINSG ELDGLENEAA ISKAIELLES KGAGEKKVNY KLRDWLFSRQ
     RYWGEPIPII HWEDGSMTTV PEDELPLLLP ETDEIKPSGT GESPLANIDA FVNVIDEKTG
     MKGRRETNTM PQWAGSCWYY LRYIDPHNEK MIADPEKLKH WLPVDLYIGG VEHAVLHLLY
     ARFWHKVLYD LGVVPTKEPF QKLYNQGMIL GEGNEKMSKS KGNVINPDDI VASHGADTLR
     LYEMFMGPLD AAIAWSEKGL DGSRRFLDRV WRLIITDENS INKKIVDSNN HSLDKVYNQT
     VKKVTEDFDT LSFNTAISQL MVFINECYKT NEVYKPYIEG FVKMLSPIAP HIGEELWDRL
     GHENTITYQP WPTFDESLLV DDEVEIVVQV NGKVRAKINI PKDLSKEEMQ DLALSNDNVK
     MSIEGKEVKK VIAVPQKLVN IVAK