ID   SYL_SYMTH               Reviewed;         861 AA.
AC   Q67SB4;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=STH444;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD39429.1; -; Genomic_DNA.
DR   RefSeq; WP_011194578.1; NC_006177.1.
DR   AlphaFoldDB; Q67SB4; -.
DR   SMR; Q67SB4; -.
DR   STRING; 292459.STH444; -.
DR   KEGG; sth:STH444; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000417; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152101"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           588..592
FT                   /note="'KMSKS' region"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  97335 MW;  CF32ACCC54E5F2F9 CRC64;
     MAEERFDFRE AEPRWQRRWD EEGIYKVERD LSRPKYYALA MFPYPSGKLH MGHVRNYTIV
     DVIARYRRMK GYNVLHPMGF DSFGMPAENA AIQHGANPAV WTRENIAEMT AQLKQMGYSY
     DWSRAVYTYR EDYYRWTQWL FLQFYKKGLA YKKTAPVNWC PSCQTVLANE QVEDGRCWRC
     DSVVTKKDLA QWFFRITQYA DELLEDLKLL EGGWPEQVRI MQQNWIGRSE GARVEFTLEA
     TGDKIPIFTT RPDTIYGVTF MVVAPEHPIV EKICTSGLIP EERVAAIRAF QEKMKHLSEI
     ARTSTEAEKE GLYTGLDVIN PFNGEKAQLW IANYVLMDYG TGAVMGVPAH DQRDFEFAQK
     YGLPVKVVIQ NPEGTLRAEE MTAAYVEPGI MVNSGPFDGT PNLEGIPKVI AYAEEQGFGQ
     KTVSYRLRDW LISRQRAWGA PIPIVYCDKC GTVPVPEKDL PVRLPDDLDF TGEGGSPLAR
     HEGFVNTTCP QCGGPARRET DTMDTFVCSS WYFLRYTDPQ NAERPWNRED VDYWMPVDQY
     VGGIEHAVLH LLYARFFTKV LRDMGLVKVD EPFARLLTQG MVLKDGSKMS KSKGNTVSPE
     EMIAKYGADA VRLFIMFAAP PERDLDWSDA GIEGAARFVN RFYRMVVSAL PAYQHARSLL
     PINPADPASV MGALSEAEIA EGLAKAAPNL TAEDRELRRV IHATVKRITA DLHDRFAFNT
     AISGLMEMTN AIYAYREKQH AEQNTSALVL AEAVQKAVLI IAPFCPHLAD ELWSRMGHPR
     SIHLEPWPAY DEEVAKADTV EIVVQINGRV RDRLEVPAGI SAAEMEAVAM ASEKVQALVA
     GKQIVKVVPV PGKLVNIVVK G
//