ID   SYL_HELAH               Reviewed;         806 AA.
AC   Q17YZ0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=Hac_0293;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(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}.
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DR   EMBL; AM260522; CAJ99136.1; -; Genomic_DNA.
DR   RefSeq; WP_011577251.1; NC_008229.1.
DR   AlphaFoldDB; Q17YZ0; -.
DR   SMR; Q17YZ0; -.
DR   STRING; 382638.Hac_0293; -.
DR   EnsemblBacteria; CAJ99136; CAJ99136; Hac_0293.
DR   KEGG; hac:Hac_0293; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; HACI382638:HAC_RS01310-MON; -.
DR   Proteomes; UP000000775; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334762"
FT   MOTIF           38..48
FT                   /note="'HIGH' region"
FT   MOTIF           572..576
FT                   /note="'KMSKS' region"
FT   BINDING         575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  93375 MW;  DA69A1CB76384ED2 CRC64;
     MDFVSIEKKW QEFWHQNESF EPKDDFNLPK KYILSMLPYP SGEIHMGHVR NYTIGDALVR
     YYRLHHYNVL HPMGFDSFGM PAENAAIKHG IHPKTWTYEN IENMQKEFEA LGFSFSKNRE
     FATSDPNYTE FEQQFFIDLW EKGLIYRKKA MLNWCPNDKT VLANEQVIEG RCWRCDTEVV
     QKELYQYYLK ITNYAEELLK DLETLKNHWP SQVLLMQKNW IGKSSGLQFR FKIADECLKA
     CNDIQEIEVF TTRADTIYGV TYIAIAPEHP LVEHAIKQVN QEDLKTIKAI LNTTPRERTL
     EKKGAFLGIY AIHPLTKQKI PIWVANFALA NYGSGALMGV PACDERDFEF ANLYHIPIKV
     ITQSPQNLPH TKEETLKNSG EWSDLPSSVA REKIIAYFEK ENLGKRVINY RLQDWGVSRQ
     RYWGAPIPMI HCKNCGIVPE TQLPVTLPED IVIDGEGNPL EKHASWKFTQ CPKCHKDALR
     ETDTMDTFIQ SSWYFLRYTT PKNQRENQAF DKNYLKYFMP VDTYIGGIEH AILHLLYARF
     FTKALRDLGY IDLDEPFKQL ITQGMVLKDG VKMSKSKGNV VSPKEILKKY GADAARLFIL
     FAAPPAKELE WNDSALEGAH RFIKRLYDKA NAINPTTYKP EFKEANLNEA EKLARKKVYE
     ALKKSHEIFN NPESTYAFNT LIASCMEALN ALNTQNNERI LCEGYFVLLQ VLEPMIPHTA
     WELSERLFKR ANFKPITIDE SALIEDSMTL ALTINGKRRA ELKVHINASK EEILALAKKE
     LEKYLENASV KKEIYVPNKL VNFVIA