ID   SYL_WIGBR               Reviewed;         864 AA.
AC   Q8D333;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=WIGBR1680;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24314.1; -; Genomic_DNA.
DR   RefSeq; WP_011069972.1; NC_004344.2.
DR   AlphaFoldDB; Q8D333; -.
DR   SMR; Q8D333; -.
DR   STRING; 36870.25166123; -.
DR   PRIDE; Q8D333; -.
DR   EnsemblBacteria; BAC24314; BAC24314; BAC24314.
DR   KEGG; wbr:leuS; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000562; 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; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152117"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   864 AA;  102169 MW;  62C8A9BD84031F3F CRC64;
     MKKEYSCKEI ERFVQKHWEI NDTFKVLEDS KKDKYYCVSM MPYPSGKLHM GHVRNYVLGD
     VIARYQRMLG KNVLHPIGWD AFGLPAETAA INNKISPEKW TISSIEYMKN QLKLLGCSYD
     WSREIITCDP KYYKWEQLLF TKLYNKNKAY KKKSIVNWCP KDKTVLANEQ VIDNLCWRCS
     SNIEMKKIFQ WFIKITDYAD ELLNDLNDLK LWPKKVKVMQ RNWIGKSKGI DVLFHIKDTN
     EKILIYVSKL EIFMGITFIV ISKEHKLIKF IENKLPSIAK LIKNYNNEKT LELNLRKKTK
     DGIFTSLFAI HPISKKILPI WISNFFFTNN DIYQSIAAIP AYNKNELDFA KKYNLPIRYV
     IKDYFEKIID FKKYNNLKEG ILFNSNIFNG LNLKNGYDRI SKFLISNKIG KRSTHYKLRD
     WCISRQRYWG APIPVLITKE NKILVVSENE LPVILPKAKN NNIIHSLNSY KDWIYVLNDN
     KLVKREVDTF DTFMESSWYL HRYTCTKYTK DILDPNATNY WFPVDQYIGG IEHATMHLLY
     LRFYHKILRD MNFVKCDEPV NRLLCQGMVL SDTFYYFSKS GNKIWTSPKN KNFERNKDNK
     IINAIDSLGN KLTHIGMSKM SKSKNNGVDP QGIINKYGSD TLRLFIMFAA PPELSLEWSD
     KGIIGANRFI KKLWKITYNY LNLKKNNNYV FYKKLKEQDN ILLEKSFYVI NKVTKDIDKN
     QTFNTAIAEI MKLTNHLNSY INKNEYNNIS IIKKVLMIII RLLYPFIPHV CFVLWNEINK
     NNDIDKTKWP KIKMPFIKNK KKNIVVQING KLKTVISFDI SCNEFLIKKC VIENNKIKNL
     LNKKKIKNII YVKNKIINIV LDDK