ID   SYL_CLOK5               Reviewed;         811 AA.
AC   A5N399;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-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=CKL_3605;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK35595.1; -; Genomic_DNA.
DR   RefSeq; WP_012103927.1; NC_009706.1.
DR   AlphaFoldDB; A5N399; -.
DR   SMR; A5N399; -.
DR   STRING; 431943.CKL_3605; -.
DR   EnsemblBacteria; EDK35595; EDK35595; CKL_3605.
DR   KEGG; ckl:CKL_3605; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002411; 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; 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; 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..811
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334745"
FT   MOTIF           38..49
FT                   /note="'HIGH' region"
FT   MOTIF           570..574
FT                   /note="'KMSKS' region"
FT   BINDING         573
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   811 AA;  93287 MW;  4F9A8EF4DF120AC5 CRC64;
     MYSTKTDKKW QQKWDQTNIY TFDEKKSSKK LYTLEMFSYP SGSNLHAGHW FNYAPVDSWA
     RMKRMQGYNV FQPMGFDAFG LPAENYAIKT GIHPKDSTEK NIDTMEKQLK SMGAMFNWEN
     EVVTCRPDYY KWNQWLFLQL YKHDLAYRKN APVNWCPSCN TVLANEQVKE GECERCGTEV
     TKKDLTQWFF KITDYTEELL KDLDNIDWPE KTKAMQRHWM GKSTGTDVTF KVADSDIKFN
     VFTTRVDTLF GVTYVVISPE NDLVDSVTKE EYKEEIEKYR EAAKKQTDIE RQSITREKTG
     VSTGSYAINP INGRKVPIWI GDYVLNTYGT GAVMAVPAHD ERDFEFATKY KLPIERVIEG
     GSSLPYVEYG KMINSDKFNG LYTPEGKEAV TKELENIGLG SGKTNYRLRD WLVSRQRYWG
     TPIPIIYCKK CGTVPVPESD LPVELPYNVQ FSPDGKSPLL KSEEFMNTTC PICGEPAKRE
     ADTLDTFVCS SWYYLRYADN KNTEKAFDKD KINKLLPVDM YVGGPEHACM HLLYARFITK
     ALRDMGFLNF DEPFLSLRHQ GLILGPDGQK MSKSKGNTIS PDDCIQKYGS DVFRMYLMFG
     FDYAEGGAWN DDGIKSMSKF VDRIERIVGN IKELINSGKN FKNSMDAAEK ELNYSRNYSI
     KSVSEDAGKF QFNTAIARIM EFTNSLYKYI QEDTKNISLL KDTILDFIKI IAPFAPHFAE
     EQWEVLGQKY SIFNEKWPEF DPKALVKEEV EIAIQINGKI KAKINIPTNL SDEQIKELSI
     SNDNIKPLLE GKNIKKVIVV KGRLVNIVVK P