ID   SYL_HAES1               Reviewed;         860 AA.
AC   Q0I5C5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=HS_1557;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(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; CP000436; ABI25825.1; -; Genomic_DNA.
DR   RefSeq; WP_011609703.1; NC_008309.1.
DR   AlphaFoldDB; Q0I5C5; -.
DR   SMR; Q0I5C5; -.
DR   STRING; 205914.HS_1557; -.
DR   PRIDE; Q0I5C5; -.
DR   EnsemblBacteria; ABI25825; ABI25825; HS_1557.
DR   KEGG; hso:HS_1557; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
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_1000009350"
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;  98111 MW;  B5297172D5A0BEE0 CRC64;
     MQEQYRPDLI EADVQKYWAE KKTFKAVKDP SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMNG KNVLQPMGWD AFGLPAEGAA IKNKTAPAKW TYENIEYMKN QLKVLGFGFD
     WDREITTCKP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD
     TPVEQKEIPQ WFIKITDYAE QLLSDLDQLP EWPDMVKTMQ RNWIGRSEGV EITFNVAHSD
     QTLTVYTTRP DTFYGVSYLA VAAAHPLAES AAKNNPELAA FIHEAKNTKV AEAELATMEK
     KGMATGLYAV HPMTGKQLPI WVANFVLMHY GTGAVMAVPA HDQRDYEFAQ KYQLPLFPVI
     KPADNSAWDF SKQAYTEHGI TINSAEFDGL DFEATFNGIA DKLEKIGVGK RQVNYRLRDW
     GVSRQRYWGA PIPMLTLENG DVVVAPLQDL PIVLPEDVVM DGVKSPIKAD PEWAKTTYNG
     QAALKETDTF DTFMESSWYY ARYTSPQYQQ AMLDADEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGFVTSDEPS KKLLCQGMVL ADAFYYTSPT NERIWVSPTK VTLERDEKGR
     IIKAVDDEGH ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGANRFL RRLWNLVFEY NQNPAQTALD PTALSVEQKA LRRDVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLTKAS LSNEQDRAVM AEALNAVVRM LYPITPHICF QLWQDLGNES
     TIDFAPWVIA DAEAMVEDEK LVVIQVNGKV RAKVTVPADM SEDEIKQVAL AEENVQKFLN
     GLTVVKTIYV QGKLFSFVAK