ID   SYL_ECO27               Reviewed;         860 AA.
AC   B7UKT2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=E2348C_0542;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS08090.1; -; Genomic_DNA.
DR   RefSeq; WP_001339340.1; NC_011601.1.
DR   AlphaFoldDB; B7UKT2; -.
DR   SMR; B7UKT2; -.
DR   EnsemblBacteria; CAS08090; CAS08090; E2348C_0542.
DR   KEGG; ecg:E2348C_0542; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000008205; 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.
FT   CHAIN           1..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199201"
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;  97234 MW;  581E890136DE0C48 CRC64;
     MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIAYMKN QLKMLGFGYD
     WSRELATCTP EYYRWEQKFF TELYKKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
     TKVERKEIPQ WFIKITAYAD ELLNDLDKLD HWPDTVKTMQ RNWIGRSEGV EITFNVNDYD
     NTLTVYTTRP DTFMGCTYLA VAAGHPLAQK AAENNPELAA FIDECRNTKV AEAEMATMEK
     KGVDTGFKAV HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS KYGLNIKPVI
     LAADGSEPDL SQQALTEKGV LFNSGEFNGL DHEAAFNAIA DKLTAMGVGE RKVNYRLRDW
     GVSRQRYWGA PIPMVTLEDG TVMPTPDDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
     MPALRETDTF DTFMESSWYY ARYTCPQYKE GMLDSKAANY WLPVDIYIGG IEHAIMHLLY
     FRFFHKLMRD AGMVNSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR
     IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE
     SGVEGANRFL KRVWKLVYEH TAKGDVAALN VDALTEDQKA LRRDVHKTIA KVTDDIGRRQ
     TFNTAIAAIM ELMNKLAKAP TDGEQDRALM QEALLAVVRM LNPFTPHICF TLWQELKGEG
     DIDNAPWPVA DEKAMVEDST LVVVQVNGKV RAKITVPVDA TEEQVRERAG QEHLVAKYLD
     GVTVRKVIYV PGKLLNLVVG