ID   SYL_YERE8               Reviewed;         860 AA.
AC   A1JQ25;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=YE2996;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL13035.1; -; Genomic_DNA.
DR   RefSeq; WP_011816835.1; NC_008800.1.
DR   RefSeq; YP_001007185.1; NC_008800.1.
DR   AlphaFoldDB; A1JQ25; -.
DR   SMR; A1JQ25; -.
DR   STRING; 393305.YE2996; -.
DR   EnsemblBacteria; CAL13035; CAL13035; YE2996.
DR   KEGG; yen:YE2996; -.
DR   PATRIC; fig|393305.7.peg.3191; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000642; 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   Gene3D; 3.90.740.10; -; 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; 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.
FT   CHAIN           1..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009467"
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   860 AA;  96934 MW;  4674AB8963DD9555 CRC64;
     MQEQYRPEDI ETQVQLHWQE KQTFKVTEDT SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIEYMKN QLKLLGFGYD
     WDREIATCSP DYYRWEQWFF TKLYEKGMVY KKTSAVNWCP HDLTVLANEQ VIDGCCWRCD
     TKVERKEIPQ WFIKITDYAD QLLNDLDTLE SWPEQVKTMQ RNWIGRSEGV DIVFNVADSE
     EKLSVYTTRP DTFMGVTYVA VAAGHPLSLQ AAATNPALAD FVAECRNTKV AEAEMATMEK
     KGMATGLYAI HPLTGEKLPI WAANFVLMDY GTGAVMAVPG HDARDWEFAT KYNLPIKPVI
     LAADGSEPDL SQEAMTEKGI LFNSGEFDGL NYEDGFNAVA DKLVALGVGQ RKVNYRLRDW
     GVSRQRYWGA PIPMVTLEDG TVVPTPEDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
     VPGLRETDTF DTFMESSWYY ARYTCPQFDK GMLDPAAANY WLPVDQYVGG IEHAIMHLMY
     FRFFHKLLRD AGLVDSDEPA KRLLCQGMVL ADAFYYSGSN GERIWVSPVD AIVERDDKGR
     IIKATDAEGH ELVYAGMSKM SKSKNNGIDP QVMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGANRFL KRVWRLAYDH TAKGATAPLD VANLTEEQKS LRRDLHKTIA KVTDDVGRRQ
     TFNTAIAAVM ELMNKLGRAP QETEQDRALL QEALLAVVRM LYPFTPHVCF SLWQALGGEG
     DIDTAPWPVA DEQAMVEDSK LVVVQVNGKV RGRITVPADA TEQQVRERAG QEHLVAKYLD
     GVTVRKVIYV PGKLLNLVVG