ID   SYL_HELHP               Reviewed;         830 AA.
AC   Q7VIY7;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=HH_0465;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77062.1; -; Genomic_DNA.
DR   RefSeq; WP_011115307.1; NC_004917.1.
DR   AlphaFoldDB; Q7VIY7; -.
DR   SMR; Q7VIY7; -.
DR   STRING; 235279.HH_0465; -.
DR   GeneID; 82135073; -.
DR   KEGG; hhe:HH_0465; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002495; 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; 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; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
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; Reference proteome.
FT   CHAIN           1..830
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152025"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           596..600
FT                   /note="'KMSKS' region"
FT   BINDING         599
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   830 AA;  95681 MW;  CC08CB32DA94E06F CRC64;
     MQERKYNPKD IESKWQQFWT EHKSFEPFDI DIATSDSMKK KYILSMFPYP SGAIHMGHVR
     NYCIGDALAR NYRQNGYNVL HPMGWDAFGM PAENAAIKHK THPKTWTYSN IDTMRKELAT
     LGLSFSKERE FATSDAIYTR FEQEFFIKMW ERGLIYRKEA YLNWCPKDKT ILANEQVIEG
     KCWRCDTPVV QKQMFQYYIK ITDYADELLE CLNKLEGHWP SQVLSMQRNW IGKSKGLSFT
     FDFSVDSLQK LGNGKVKLEV FTTRPDTIYG VTYCAVAPEH PIVQQLIENK SLDESVIKSI
     EAIKNTTARA RAMSEKVGFD LGVYVIHPLT QEKLPVWVAN FVLMDYGSGA VMSVPMHDER
     DFEFAKTYAL PFKCVLTKEI DGEEPTQEIC AAYEEGFLIN SGEFSGMSSS QAKERIIAHF
     ENASIGKGIT NYRLRDWGVS RQRYWGAPIP MVHCQSCGIV PEKIENLPIT LPEDVVIDGE
     GNPLDKHLVW KDCLCPKCGK KAQRESDTMD TFIQSSWYFL RYSTPRKLWE KQAFDKESLT
     YWLNVDEYIG GIEHAILHLL YARFWTKVLR DLGYIEIDEP FANLLTQGMV LKDGAKMSKS
     KGNIVNPNEL IAHYGADTAR LFVLFAAPPT RELEWNDKAV EGAHRFLKRL WERAEHIESC
     TQKPHINHKT LQKNEQYARQ KVYEALQKSN EIFSKKQSGY AFNTLIAASM EAFNALNEQE
     NPLVWTEGYF VLLHILEPIV PHICWELSEQ YFRRCNFAPL SVDKDALTKE SVIYAITING
     KKRAEVEMPL GLSKEEIIIQ AKESVPKWLE GVEILKEIIV PNKLVNLVVK
//