ID SYL_CLOD6 Reviewed; 806 AA.
AC Q182K8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=CD630_25210;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(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; AM180355; CAJ69408.1; -; Genomic_DNA.
DR RefSeq; WP_003416419.1; NZ_JAUPES010000003.1.
DR RefSeq; YP_001089035.1; NC_009089.1.
DR AlphaFoldDB; Q182K8; -.
DR SMR; Q182K8; -.
DR STRING; 272563.CD630_25210; -.
DR EnsemblBacteria; CAJ69408; CAJ69408; CD630_25210.
DR KEGG; cdf:CD630_25210; -.
DR KEGG; pdc:CDIF630_02772; -.
DR PATRIC; fig|272563.120.peg.2661; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR PhylomeDB; Q182K8; -.
DR BioCyc; PDIF272563:G12WB-2676-MONOMER; -.
DR Proteomes; UP000001978; 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 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..806
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091308"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 566..570
FT /note="'KMSKS' region"
FT BINDING 569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 806 AA; 92433 MW; 48AEB19A0A21102C CRC64;
MSVYNFKEVE SKWQKIWKDN NQYKMDTAQT EKPNYYTLEM FPYPSGKIHM GHVRNYSIGD
VVARFKKMEG YNVLHPMGWD SFGLPAENAA IKHGIHPHKW TMENIEEMKE QLNLLGISYD
WDKEVATSTP EYYRFTQEIF LKFLEHGLAY KKKSYVNWCP SCETVLANEQ VVQGACERCK
ATVLKKDLEQ WYFKTTEFAE ELLNDLDTLD GWPEKVKTMQ KNWIGKSTGA DLVFDIDGTD
KSMTVFTTRP DTTYGVTYMV LAPEHELVKE LVAGTEYEAD VEAFVQKMHT MTEIERTAAD
VEKEGMFIGR YVINPLNGKK VPLWIANYVL VEYGTGAIMA VPAHDERDRD FAEKYNLDII
DVITEDNKMI NSEEFNGLDA SEGFEGIIDK LEKEGRGKRT INYRLRDWLV SRQRYWGCPI
PVVYCDECGI VPVKKEDLPV LLPTDVEFTG KGESPLTTSK QFMSTTCPHC GKPARREVDT
MDTFVDSSWY FLRYVDSNNE NEPFSKELVN RWHPVDQYIG GVEHAIMHLL YARWFVKAFK
SMGMVDFNEP FKNLLTQGMV LMDGSKMSKS KGNTVSPMDI IDEYGADTAR LFVLFAAPPE
RDLDWSEQGV DGCFRFLNRV YRLVDELADV VKKDVEFGEL NSQDKDMRYT IHSTLKKVTA
DLSEKFGFNT AISALMELIN DMYKYKELDN INEAVIKEGV QTIVTIIAPF APHLGEELWT
MIGKEGSVFD IDWPKYDEKA LVKDEIEVVV QVNGKVRGKL TVNSNISKDE MEKVALEDEK
IKGLVEGKTI VKVVAVPKKL VNIVVK
//
