ID   SYL_HELPJ               Reviewed;         806 AA.
AC   Q9ZJ63;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 142.
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=jhp_1452;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD07021.1; -; Genomic_DNA.
DR   PIR; G71805; G71805.
DR   RefSeq; WP_000345685.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJ63; -.
DR   SMR; Q9ZJ63; -.
DR   KEGG; hpj:jhp_1452; -.
DR   PATRIC; fig|85963.30.peg.1091; -.
DR   eggNOG; COG0495; Bacteria.
DR   Proteomes; UP000000804; 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_0000152027"
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;  93212 MW;  CE1BF5967AF21466 CRC64;
     MDFINIEKKW QEFWWKNKSF EPKDDFNLPK KYILSMLPYP SGEIHMGHVR NYTIGDALAR
     YYRLHHYNVL HPMGFDSFGM PAENAAIKHG IHPKTWTYEN IEAMQKEFEA LGFSFSKNRE
     FATSDPDYTK FEQQFFIDLW EKGLIYRKKA MLNWCPNDKT VLANEQVIDG RCWRCDTEVI
     QKELYQYYLK ITNYAEELLK DLETLENHWP SQVLTMQKNW IGKSSGLQFG FKIADECLKA
     CNNIQEIEVF TTRADTIYGV TYIAIAPEHP LVEHAIKRVS QEDSKMIKAI LNTTQRERAL
     EKKGAFLGIY AIHPLTKQKI PVWVANFALA NYGSGALMGV PACDERDFEF ANLYHIPIKV
     ITQSPQNLPH TKEEILKNSG EWSDLSSSVA REKIIAYFEK ENLGKRVINY RLQDWGVSRQ
     RYWGAPIPMI HCKHCGIVPE TQLPVTLPED IVIDGEGNPL EKHASWKFAQ CPKCHKDALR
     ETDTMDTFIQ SSWYFLRYTT PKNQRENQAF DQNYLKYFMP VDTYIGGIEH AILHLLYARF
     FTKALRDLGY LHLDEPFKQL ITQGMVLKDG AKMSKSKGNV VSPKEILKKY GADAVRLFIL
     FAAPPAKELE WNDNALEGAH RFIKRLYDKA NAITPTTSKP EFKEVGLNEA QKLARKKVYE
     ALKKSHEIFN KAESAYAFNT LIASCMEALN ALNAQSDEQI LCEGYFVLLQ ILEPMIPHTA
     WELSERLFKR ENFKPIEVDE SALIEDFMTL GLTINGKRRA ELKVNINASK EEIIILAKKE
     LEKYLENASV KKEIYVPNKL VNFVTA
//