ID   SYL_HISS2               Reviewed;         860 AA.
AC   B0URM9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=HSM_0467;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000947; ACA32112.1; -; Genomic_DNA.
DR   RefSeq; WP_012341304.1; NC_010519.1.
DR   AlphaFoldDB; B0URM9; -.
DR   SMR; B0URM9; -.
DR   STRING; 228400.HSM_0467; -.
DR   EnsemblBacteria; ACA32112; ACA32112; HSM_0467.
DR   KEGG; hsm:HSM_0467; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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_1000074836"
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;  98163 MW;  2CE05913359BC5AB CRC64;
     MQEQYRPDLI EADVQKYWAE KKTFKAVKDP FKEKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMNG KNVLQPMGWD AFGLPAEGAA IKNKTAPAKW TYENIEYMKN QLKVLGFGFD
     WDREITTCKP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGGCWRCD
     TPVEQKEIPQ WFIKITDYAE QLLSDLDQLP EWPDMVKTMQ RNWIGRSEGV EITFNVAHSD
     QTLTVYTTRP DTFYGVSYLA VAAAHPLAEN AAKNNPELAA FIHEAKNTKV AEAELATMEK
     KGMATGLYAV HPMTGKQLPI WVANFVLMHY GTGAVMAVPA HDQRDYEFAQ KYQLPLFPVI
     KPADNSAWDF SKQAYTEHGI TINSAEFDGL DFEATFNGIA DKLEKIGVGK RQVNYRLRDW
     GVSRQRYWGA PIPMLTLENG DVVVAPLQDL PIVLPEDVVM DGVKSPIKAD PEWAKTTYNG
     QVALKETDTF DTFMESSWYY ARYTSPQYQQ AMLDADETNY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGFVTSDEPS KKLLCQGMVL ADAFYYTSPT NERIWVSPTK VTLERDEKGR
     IIKAVDDEGH ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGANRFL RRLWNLVFEY NQNPAQTALD PTALSVEQKA LRREVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLTKAS LSNEQDRAVM AEALNAVVRM LYPITPHICF QLWQDLGNES
     AIDFAPWVIA DAEAMVEDEK LVVIQVNGKV RAKVTVPADM SEDEIKQVAL AEENVQKFLN
     GLTVVKTIYV PGKLFSFVAK