ID   SYL_CLOB1               Reviewed;         813 AA.
AC   A7FPP5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=CLB_0226;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(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; CP000726; ABS34298.1; -; Genomic_DNA.
DR   RefSeq; WP_011948005.1; NC_009697.1.
DR   AlphaFoldDB; A7FPP5; -.
DR   SMR; A7FPP5; -.
DR   GeneID; 5187707; -.
DR   KEGG; cba:CLB_0226; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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_1000009325"
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;  92912 MW;  F4DECBDF3244DC0D CRC64;
     MGNYSTKIDE KWQKKWEENS LYKFNNKNLD 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 YGGMVNSGEF DGLLGNEAKE 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 YLGIDAIKNA LFLRESIIDF ITLLAPFAPH
     FAEEQWKLIG INSSIFNEKW PEFDPKALIK DEVEIAVQVN GKIRAKINIS TSSSEDEIKE
     SALNNEDIKN SIGDKEIKKV IVIKNRLVNI VAK