ID   SYL_NATTJ               Reviewed;         826 AA.
AC   B2A6C2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=Nther_0537;
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001034; ACB84133.1; -; Genomic_DNA.
DR   RefSeq; WP_012447019.1; NC_010718.1.
DR   AlphaFoldDB; B2A6C2; -.
DR   SMR; B2A6C2; -.
DR   STRING; 457570.Nther_0537; -.
DR   KEGG; nth:Nther_0537; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   InParanoid; B2A6C2; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001683; 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..826
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091337"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   826 AA;  95481 MW;  7FE2F0098DB072CC CRC64;
     MKEYQPQKIE SKWQKRWQDE ISYETEVDHN KDKYYVLEMF PYPSGKLHMG HMRVYSIGDV
     LARFQRMRGY NVLHPMGWDA FGLPAENAAI ENQDLPSRWT YANIDNMKDQ LQALGTSYDW
     KREVSTCSPD YYKWTQWMFL QLYKNGLAYK KKAPVNWCPE CETVLANEQV ENGACWRCDS
     MVEQKQLSQW FFKITEYADR LDQDLELLEE WPDRVKTMQK NWIGKSQGTE IDFPVKGSRE
     KIRAFTTRPD TIFGATYMVL APEHPMTEQL VQGTDQEKEV MDFIKGVHEM GKEAREAEDL
     EKEGVFTGRW AINPLNGEEI PILVGNYVLM EYGTGAIMAV PAHDQRDFQF AHKYNLPIKE
     VVTPPEGEGK TESETHDELK KAYTDHGILI NSPGYNGMTS EQAIEQITRD IENKGIGAGV
     TTYRLRDWLV SRQRYWGAPI PVLYCDQCGI LPVPEDELPV QLPEDVDFSQ GSRNVLAARQ
     DFVETSCPQC GGSAQRETDT MDTFVCSSWY FLRYTTPWDN EVPFRQEDVN YWMPVDQYIG
     GIEHAVLHLL YARFFTKVMY DQGYTNFKEP FSRLLAQGMV NKDGAKMSKS KGNVVSPDEI
     LRTYGADTGR LFILFAAPPE KDLDWNDEGV EGCYRFLQRL YRLVNDNQNL VDLQLDDTKF
     TKEDKEYHRL IHKTIKKVTD DISERHNFNT AISAIMELTN ASSKYKEQKE VNESLLRTGL
     ETIVMLLAPF TPHIAEELWE TLGYQDSVHK LNWPSYDEKA MVAEEAEMVV QVNGKVRDHL
     TVPADSSEET IKEKALEREK VQKYISGAEI KKVIVIPQKL VNIVCK
//