ID   SYL_CLOPE               Reviewed;         816 AA.
AC   Q8XML8;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=CPE0670;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB80376.1; -; Genomic_DNA.
DR   RefSeq; WP_011009963.1; NC_003366.1.
DR   AlphaFoldDB; Q8XML8; -.
DR   SMR; Q8XML8; -.
DR   STRING; 195102.gene:10489931; -.
DR   EnsemblBacteria; BAB80376; BAB80376; BAB80376.
DR   KEGG; cpe:CPE0670; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000818; 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; Reference proteome.
FT   CHAIN           1..816
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152003"
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   816 AA;  92664 MW;  83C2FD5A75D0DF07 CRC64;
     MGNYSTAIDK KWQDKWAESG LYKFDPNKEG EKLYVLEMFS YPSGSQLHAG HWFNYGPVDS
     WARFKRMQGY NVFQPMGFDA FGLPAENFAI KTGIHPQDST IKNIAKMEEQ LKAMGAMFNW
     ENEVVTCSPE YYKWTQWLFL KLYEKGLAYR KKAPVNWCPS CQTVLANEQV VDGACERCST
     EVTKKDLTQW FFKITDYADE LLDKLDGLDW PEKTVSMQKH WIGRSTGSQV NFKVKDSDLN
     FDVFTTRVDT LCGVSYVVLA PENPLVDEIV SAEQKEAVEN YKEEAKKQSD IERQSISREK
     TGVFTGAYAI HPLTGKEVPI WVGDYVLATY GTGAVMAVPA HDERDFAFAE KFNLPINRVI
     EAKDGSETNL PFCEHGILVN SGEFDGLTTD EAKEKIVEKL SSMGLGEKKV NFRLRDWLVS
     RQRYWGAPIP VVYCEECGIV PVPESQLPVE LPYDVEFAPD GKSPLAKSEA FVNTTCPHCG
     KPAKRETDTL DTFVCSSWYY LRYPDNKNTE APFNPELINK MLPVDKYVGG PEHACMHLLY
     ARFITKALRD MGYLNFDEPF TSLTHQGLIL GPDGLKMSKS KGNTISPDDY IKEYGADVFR
     MYLMFGFAYT EGGAWSDDGI KSVNRFVERI ERIIDTAREA ISKGENNKTT MDKAEKELNY
     WRHNTIKSVT DDTDKLQFNT AIARMMEFIN ALSKYTQEKE MNLDFLKDVV SDYLRLLAPF
     APHFSEEQWN LLGNSYSIFN EAWPKFDPKA LVKDEVEIAI QVNGKIKNKI MVSSDLDEEG
     IKAAALADEK IIASTEGKTV VKVIVIKGRL VNIVVK