ID   SYL_CAMJJ               Reviewed;         809 AA.
AC   A1W078;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=CJJ81176_1109;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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; CP000538; EAQ72112.1; -; Genomic_DNA.
DR   RefSeq; WP_002855948.1; NC_008787.1.
DR   AlphaFoldDB; A1W078; -.
DR   SMR; A1W078; -.
DR   KEGG; cjj:CJJ81176_1109; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   Proteomes; UP000000646; 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; cd07958; Anticodon_Ia_Leu_BEm; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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.
FT   CHAIN           1..809
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009318"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           579..583
FT                   /note="'KMSKS' region"
FT   BINDING         582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   809 AA;  93356 MW;  C990B140335DCC73 CRC64;
     MAYEASLIEK KWQKIWDENE YFEPKDDLNL PKKYILSMFP YPSGRIHMGH VRNYTIGDAL
     ARYYRKIGFN VLHPIGFDSF GMPAENAAIK HKIHPKSWTY ENIAYMKKEL FSLGFSFSKK
     RMLATSDPLY TKFEQEFFIK MFEKGLIYTK EANVNWCEQD QTVLANEQVE DGKCWRCGHE
     VAQKKMPGYY VKITAYAEEL LKDLEELKDK WPNQVLTMQE NWIGKSEGLE FSLNLDEESK
     QKTKESSLEV FTTRADTIYG VSYIALAPEH KIVQNLLSQN LLNQDVLNKI KAIQNQSPRE
     RQSSEKEGYF LGIYAIHPLS GEKIPLWVAN FILADYGSGA VMAVPAHDER DFEFATKYNL
     AIKQVIQTQE NLPYTQKSGK LIHSQEFDNL DCNEARLKII SQFEAKNIGK RVVNFKIRDW
     GVSRQRYWGA PIPMIKCQSC GIVPQKLENL PITLPEDVQI TGEGNPLDKH PTWKNCICPK
     CGKEAQKESD TLDTFFESSW YFARFASDEK TWQEKALDEK SVKYWMSVDQ YIGGIEHAIL
     HLLYARFFQK ALRDLGYLTQ NEPFDRLLTQ GMVLKDGAKM SKSKGNVVDP DEIIEKYGAD
     TARLFILFAA PPAKELEWND DAVEGAYRFI CKLYDRAQNV KKGELVELKQ ENLNKEEKYA
     RLKVYEALKK SFEVYHQSFA FNTLIAACME ALNALALCKN EALEQEAFYI ILNILEPIIP
     HVCFELSEEL FKCKNFKKLE LKEEVFVKDT LNLAVSINGK KRAEFEISSS ASKEEILAFA
     KENTAKWLEG KSIVKEIYVE GKLVNLVIK
//