ID   SYL_CLOAB               Reviewed;         812 AA.
AC   Q97LB6;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 126.
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};
GN   OrderedLocusNames=CA_C0646;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78623.1; -; Genomic_DNA.
DR   PIR; D96979; D96979.
DR   RefSeq; NP_347283.1; NC_003030.1.
DR   RefSeq; WP_010963965.1; NC_003030.1.
DR   AlphaFoldDB; Q97LB6; -.
DR   SMR; Q97LB6; -.
DR   STRING; 272562.CA_C0646; -.
DR   GeneID; 44997157; -.
DR   KEGG; cac:CA_C0646; -.
DR   PATRIC; fig|272562.8.peg.849; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000814; 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; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..812
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152002"
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   812 AA;  92889 MW;  8556803C1FCFE29C CRC64;
     MSTYSTKVDE KWQKKWEETS LYKFDENNLE KKLYVLEMFS YPSGAKLHAG HWFNYAPVDS
     WARFKKMTGY NVFQPMGFDA FGLPAENYAI KTGIHPKDST LKNIETMEKQ LKSMGAMFNW
     DHEVITCTPD YYKWTQWLFL ELYKNGLAYR KKAPANWCPS CNTVLANEQV VDGSCERCGT
     EVIKKDLTQW FFKITNYAEE LLQKLDELDW PEKTKAMQKH WIGKSKGAEV TFKVDNSDLK
     FDVFTTRVDT LCGVTYVVLA PESPLADELT KPEYKEKVEE YKLQAQKQSE IERQSLTREK
     TGVFTGSYAI NPINNKKVPI WIADYVIYTY GTGAVMAVPS HDERDFAFAT KYDLPIVRVV
     EGGEELPFTG YGPLVNSGEF DGLKGNKAKE AIVSKLSEND LGRWKVNYRL RDWLVSRQRY
     WGAPIPVVYC EKCGIVPVPE KDLPVELPYN VEFNPTGKSP LTTSEEFMNT TCPHCGGHAT
     RESDTLDTFV CSSWYYLRYA DNENSDAPFD KEKISKMLPV DKYVGGPEHA CMHLLYARFI
     TKALRDIGYL NFDEPFLSLR HQGLILGPDG QKMSKSKGNT ISPDDIIAEH GSDVFRMYLM
     FGFDYAEGGA WSDDGVKAMS KFVDRFSRMI ETAKEEINNP KNSKTDMGKE EKELNYVRNH
     SIKAVTEDMD KFQFNTCIAR LMEFTNSLSK YLTVDNKNIK LLKDTTIDII KLIAPFAPHF
     AEEQWNIIEE KYSVFNEKWP EFDEKALVKD EVEIAIQING KIKAKINIAT NLSEDEIKSA
     ALADDKVKAA TDGKNIVKVI VIKGRLVNIV VK
//