ID   SYL_CLOBL               Reviewed;         813 AA.
AC   A7G9T9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CLI_0249;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) 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; CP000728; ABS39371.1; -; Genomic_DNA.
DR   RefSeq; WP_011987262.1; NC_009699.1.
DR   AlphaFoldDB; A7G9T9; -.
DR   SMR; A7G9T9; -.
DR   PRIDE; A7G9T9; -.
DR   EnsemblBacteria; ABS39371; ABS39371; CLI_0249.
DR   KEGG; cbf:CLI_0249; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002410; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..813
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009327"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           572..576
FT                   /note="'KMSKS' region"
FT   BINDING         575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   813 AA;  93072 MW;  A6D241BCDEBEEC0D CRC64;
     MGNYSTKIDE KWQKKWEENS LYKFNNDNLD KKLYVLEMFS YPSGSKLHAG HWFNYGPVDS
     WARFKRMQGY NVFQPMGFDA FGLPAENYAI KTGIHPKDST FKNIETMETQ LKAMGAMFNW
     ENEVITCSPD YYKWTQWLFL KLYEKGLAYK KKAPVNWCPS CNTVLANEQV LDGKCERCDS
     NVDKKNLEQW FLKITDYADE LLEKLDELDW PEKTKAMQKH WIGKSVGAEV TFNVADSDLS
     FNVFTTRVDT LFGVTYVVLA PENDLVDKLT TPENKAEVES YKTQAKNQSD IERQSITREK
     TGVFSGSYAI NPINGKKVPI WIGDYVLNTY GTGCVMAVPA HDERDFAFAT KYNLPIERVI
     EGGDSLPYTE YGKMVNSGEF DGLFGNKAKE AVISKLESMN LGRKKINYRL RDWLVSRQRY
     WGAPIPIIYC EKCGTVEVPI EQLPVELPYN VEFSPDGKSP LGKCDDFINT TCPKCGGPAK
     READTLDTFV CSSWYYLRYP DNNNEKDAFN PELINKMLPV DKYVGGPEHA CMHLLYARFI
     TKALRDMGYL NFDEPFLSLT HQGLILGPDG LKMSKSKGNT ISPDDYIKEF GADVFRMYLM
     FGFDYTEGGA WSDDAIKSIG KFVDRVERIL ENAREEIKNS KDNKSTMDKD EKELNYVRHH
     SIKSITEDID KMQFNTSIAR LMEFTNALSK YLGSDTLRNA SFLRESIIDF ITLLAPFAPH
     FAEEQWELIG INSSIFNEKW PEFDPKALIK DEVEIAVQVN GKIRAKINIY TSSSEDEIKE
     SALNNDDIKN SIGDKEIKKV IVIKNRLVNI VAK