ID   SYL_HAEI8               Reviewed;         861 AA.
AC   Q4QLY8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, 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=NTHI1090;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87959.1; -; Genomic_DNA.
DR   RefSeq; WP_011272290.1; NC_007146.2.
DR   AlphaFoldDB; Q4QLY8; -.
DR   SMR; Q4QLY8; -.
DR   EnsemblBacteria; AAX87959; AAX87959; NTHI1090.
DR   KEGG; hit:NTHI1090; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002525; 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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152024"
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   861 AA;  97671 MW;  E8365392CF2C16EF CRC64;
     MQEQYRPDMI EPKVQQYWAE NKVFKAIKDE SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPFGWD AFGLPAEGAA IKNKTAPAKW TYENIAYMKK QLQLLGFGFD
     WDREIATCKP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD
     TPVEQKEIPQ WFIKITDYAE QLLGGLDALP QWPDMVKTMQ RNWIGRSEGV EITFDVANTN
     EKVAVYTTRP DTFYGVSYLG IAAAHPLASL AAQNNSELAA FIQEAKNAKV AEADLATMEK
     KGMATGLFAI HPLTGEKLPI WVANFVLMHY GTGAVMAVPA HDQRDFEFAQ KYSLQIKQVI
     EPIADEEIDL TKQAFVEHGK LVNSAEFDGK DFDGAFNGIA DKLEKLGVGK RQVNYRLRDW
     GVSRQRYWGA PIPMLTLENG DVVPAPMEDL PIILPEDVVM DGVKNPIKAD PNWAKTTLNG
     APALKETDTF DTFMESSWYY ARYTCPQYQN GMLDAEEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGFVTSDEPA DKLLCQGMVL ADAFYYTSPT NERIWVSPTL VTLERDEKGR
     IIKATDPEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGAKRFL GRVWNLVYQY QQNPAKTSLD ITALSAEQKV LRREVHKTIA KVSDDIGRRQ
     TFNTAIAAVM ELMNKLTKAS LDSEQDRAVM AEALSAVVRM LYPITPHICF ELWQALGNES
     AIDTAEWVKA DEAAMVEDEK LIVVQVNGKV RGKVTVAADA DEDTVKTIAF ADENVKKFID
     NQHIVKVIYV VGKLLNVVVK P