ID   SYL_HELPH               Reviewed;         806 AA.
AC   Q1CR59;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
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};
GN   OrderedLocusNames=HPAG1_1496;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(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; CP000241; ABF85563.1; -; Genomic_DNA.
DR   RefSeq; WP_000345689.1; NC_008086.1.
DR   AlphaFoldDB; Q1CR59; -.
DR   SMR; Q1CR59; -.
DR   KEGG; hpa:HPAG1_1496; -.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   Proteomes; UP000008835; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_0000334763"
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;  93122 MW;  7DA8EFC45A0F5810 CRC64;
     MDFINIEKKW QEFWWKNKSF EPKDDFNLPK KYILSMLPYP SGEIHMGHVR NYTIGDALAR
     YYRLHHYNVL HPMGFDSFGM PAENAAIKHG IHPKTWTYEN IEAMQKEFEA LGFSFSKNRE
     FATSDPDYTK FEQQFFIDLW EKGLIYRKKA MLNWCPNDKT VLANEQVIDG RCWRCDTEVV
     QKELYQYYLK ITNYAEELLK DLETLEDHWP SQVLIMQKNW IGKSSGLQFG FKIADECLKA
     CNGIQEIEVF TTRADTIYGV TYIAIAPEHP LVEHAIKRVS QEDSKIIKAI LNTTQRERAL
     EKKGAFLGIY AIHPLTKQKI PVWVANFALA NYGSGALMGV PACDERDFEF ANLYHIPIKV
     ITQSLQNLPH TKEEVLKNSG EWSDLSSSVA REQIIAYFEK ENLGKRVINY RLQDWGVSRQ
     RYWGAPIPMI HCKHCGIVPE TQLPVTLPED IVIDGEGNPL EKHASWKFAQ CPKCHKDALR
     ETDTMDTFIQ SSWYFLRYTT PKNQRENQAF DQNYLKYFMP VDTYIGGIEH AILHLLYARF
     FTKALRDLGY LHLDEPFKQL ITQGMVLKDG AKMSKSKGNV VSPKEILKKY GADAARLFIL
     FAAPPAKELE WNDSALEGAH RFIKRLYDKA NAITPTTSKP EFKGVILNEA QKLARKKVYE
     ALKKSHEIFN KTESTYAFNT LIASCMEALN ALSAQNNERI LCEGYFVLLQ ILEPIIPHTA
     WELSERLFKR ENFKPIAIDE SALMEDFMTL GLTINGKRRA ELKVNINASK EEIIVLAKKE
     LEKYLEKASV KKEIYVPNKL VNFVIA
//