ID   SYL_CLOP1               Reviewed;         816 AA.
AC   Q0TTD0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=CPF_0657;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000246; ABG83404.1; -; Genomic_DNA.
DR   RefSeq; WP_003457020.1; NC_008261.1.
DR   AlphaFoldDB; Q0TTD0; -.
DR   SMR; Q0TTD0; -.
DR   STRING; 195103.CPF_0657; -.
DR   EnsemblBacteria; ABG83404; ABG83404; CPF_0657.
DR   GeneID; 29572216; -.
DR   KEGG; cpf:CPF_0657; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001823; 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..816
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009329"
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;  92693 MW;  2A5FDC10D11E5289 CRC64;
     MGNYSTAIDK KWQEKWAESG LYKFDPNKEG EKLYVLEMFS YPSGSQLHAG HWFNYGPVDS
     WARFKRMQGY NVFQPMGFDA FGLPAENFAI KTGIHPQDST IKNIAKMEEQ LKAMGAMFNW
     ENEVVTCSPE YYKWTQWLFL KLYEKGLAYR KKAPVNWCPS CQTVLANEQV VDGACERCST
     EVTKKDLTQW FFKITDYADE LLDKLDDLDW PEKTVSMQKH WIGRSTGSQV NFKVKDSDLN
     FDVFTTRVDT LCGVSYVVLA PENPLVDEIV SAEQKEAVEN YKEEAKKQSD IERQSISREK
     TGVFTGAYAI HPLTGKEVPI WVGDYVLATY GTGAVMAVPA HDERDFAFAE KFNLPINRVI
     EAKDGSETNL PFCEHGILVN SGEFDGLTTD EAKEKIVEKL ASMGLGEKKV 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
     APHFSEEQWS LLGNSYSIFN EAWPKFDPKA LVKDEVEIAI QVNGKIKNKI MVSSDLDEEG
     IKAAALADEK IIASTEGKTV VKVIVIKGRL VNIVVK