ID   SYL_SHOC1               Reviewed;         804 AA.
AC   Q5WE05;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=ABC2871;
OS   Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD65405.1; -; Genomic_DNA.
DR   RefSeq; WP_011247713.1; NC_006582.1.
DR   AlphaFoldDB; Q5WE05; -.
DR   SMR; Q5WE05; -.
DR   STRING; 66692.ABC2871; -.
DR   KEGG; bcl:ABC2871; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001168; 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   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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151972"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           574..578
FT                   /note="'KMSKS' region"
FT   BINDING         577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  91100 MW;  D97D7DA775C5AB79 CRC64;
     MSFSHQEIEK KWQAFWEENK TFKTDEQAEG PHFYALDMFP YPSGAGLHVG HPEGYTATDI
     LARMKRMQGY NVLHPMGWDA FGLPAEQYAL DTGKHPATFT KQNIDTFKRQ IKELGFSYDW
     DREISTTDPH YYKWTQWIFL KLYEKGLAYI DEVAVNWCPA LGTVLANEEI VDGVSERGGH
     PVERRPMKQW VLRITAYAER LLEDLEELEW PESLKDMQRN WIGKSEGAEV TFKINEHSVN
     VFTTRPDTLF GATYMVLAPE HKLVTEITTD EQKEAVEAYQ KQVALKSDIE RTDLAKEKTG
     AFTGAYAINP VNGEKIPVWI ADYVLISYGT GAVMAVPAHD ERDFEFANAF GLPIKEVVAG
     GDVSKAAYTG DGEHVNSDFL NGLNKQEAVE KMIVWLEENG AGQRKVTYRL RDWLFSRQRY
     WGEPIPIIHW EDGSMSALDE SELPLVLPDL EEIKPSGTGE SPLANAKDWL EVVDPKTGMR
     GRRETNTMPQ WAGSCWYYLR YIDPTNDEAL ADPEKLKNWL PVDTYIGGAE HAVLHLLYAR
     FWHKFLYDIG VVPTKEPFQK VFNQGMILGE NNEKMSKSKG NVVNPDEIIA SHGADTLRLY
     EMFMGPLDAS VAWSTNGLDG SRRFLERVWR LIVNEETGKL NSNVKDVEGN EAFVRTYHQT
     VKKVTEDFAE LRFNTGISQL MVFVNEGNKQ EVLPKALIEG FVKLLSPVAP HIAEELWEKL
     GHTDTITYEA WPTYDESLLV ENEVEVVVQM NGKVKTKLVI NKGASKEEME AAALADEKVQ
     AAIGEKTIRK VIAVPGKLVN IVVG
//