ID   SYL_NITSB               Reviewed;         815 AA.
AC   A6Q512;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=NIS_1464;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF70571.1; -; Genomic_DNA.
DR   RefSeq; WP_012082834.1; NC_009662.1.
DR   AlphaFoldDB; A6Q512; -.
DR   SMR; A6Q512; -.
DR   STRING; 387092.NIS_1464; -.
DR   KEGG; nis:NIS_1464; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   InParanoid; A6Q512; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001118; 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; 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; 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; 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..815
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009382"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           583..587
FT                   /note="'KMSKS' region"
FT   BINDING         586
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   815 AA;  94146 MW;  48FB5009F2996E89 CRC64;
     MQYDPKAIEQ KWQNEWKEKN AFEPQENYSK EKMYVLSMFP YPSGRIHMGH VRNYTIGDAI
     ARYYRKTGAN VLHPIGWDAF GMPAENAAIK HKVHPKKWTY ENIDYMRKEL DALGLSFSHD
     REFATCDPLY SKWEQSFIID MWNRGLLYRK KAAVNWCPHD KTVLANEQVI EGRCWRCDTE
     VVQKEIEQYF LKITDYAQEL LEDLKKLEGN WPNQVIAMQR NWIGRSEGLE FRLHFDETSA
     KKAGIDGFEV FTTRPDTIYG VTYTALAPEH PVVKHLIETK QLSDEAVQKI CTMQNQNART
     RQQAEKEGLF LDLYVIHPLT KQKIPVWVAN FVLAEYGSGA VMAVPAHDER DFEFAHKYNL
     PIKYIIKPKE GELDTTKAYT EPGILFDSGE FSGFESSEAK QKIIEYFEEN GIGKRSVNYK
     LKDWLVSRQR YWGTPIPLIK CPKCGIVPEK KENLPVTLPE DVEITGEGNP LELHPTWKKT
     TCPKCGGEAE RETDTLDTFV ESSWYFLRYT TPRKYWEEVP FRKEDTDYWM PVDQYIGGIE
     HAILHLLYAR FFTKVLRDLG YVNLDEPFKR LLTQGMVLKD GAKMSKSKGN TVDPDEIVAK
     FGADTARLFI LFAAPPAKEL EWSDSAVEGA YRFIKRFFER SQNAYKTKSL PKIDQKSLSK
     EEKEARKKVY EALQKSTDVY TKSFSFNTLI AASMEALNAL NGQNNPDIWT EGYWVLTNIL
     EPIIPHTCWE ISHNLFERNN FTRLQLDPAA LEEDSVTLAV TVNGKRRAEI EVPKDASKEE
     ILAKAKEIAK KWIDGKTIVK EIVVPGRLVN IVVKG
//