ID   SYL_CAMJD               Reviewed;         809 AA.
AC   A7H2R6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=JJD26997_0632;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) 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; CP000768; ABS43284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H2R6; -.
DR   SMR; A7H2R6; -.
DR   EnsemblBacteria; ABS43284; ABS43284; JJD26997_0632.
DR   KEGG; cjd:JJD26997_0632; -.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002302; 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; 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   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 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..809
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009317"
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;  93268 MW;  C537E7C634CEE377 CRC64;
     MAYEASLIEK KWQKIWDENE YFEPKDDLNL PKKYILSMFP YPSGRIHMGH VRNYTIGDAL
     ARYYRKIGFN VLHPIGFDSF GMPAENAAIK HKIHPKSWTY ENIAYMKKEL FSLGFSFSKK
     RMLATSDPLY TKFEQEIFIK MFEKGLIYTK EANVNWCEQD QTVLANEQVE DGKCWRCGHE
     VVQKKMPGYY VKITAYAEKL LKDLEGLRDK WPNQVLTMQE NWIGKSEGLA FSLNLDEKSK
     QKAKESSLEV FTTRADTIYG VSYVALAPEH KIVQNLLLQN LLNQDVLNKI KAIQNQSPRE
     RQSSEKEGYF LGIYAIHPLS GEKIPLWVAN FVLSDYGSGA VMAVPAHDER DFEFAKKYNL
     AIKQVIQTQE NLPYTQKLGK LIHSQEFDNL DCNEARLKII SQFEAKNIGK RVVNFKIRDW
     GVSRQRYWGA PIPMIKCQSC GIAPQKLENL PITLPEDVQI TGEGNPLDKH PTWKNCICPK
     CGKEAQKESD TLDTFFESSW YFARFASDEK TWQEKALDEK SVKYWMSVDQ YIGGIEHAIL
     HLLYARFFQK ALRDLGYLTQ NEPFDRLLTQ GMVLKDGAKM SKSKGNVVDP DEIIEKYGAD
     TARLFMLFAA PPAKELEWND DAVEGAYRFI CKLYDRAQNI KKGELVELKQ ENLNKEEKYA
     RLKVYEALKK SEEVYHQSFA FNTLIAACME ALNALALCKN EALEQEAFYI ILNILEPIIP
     HVCFELSEEL FKCKNFKKLE LKEEVFVKDT LNLAVSINGK KRAEFKISSS ASKEEILAFA
     KENTAKWLEG KSIVKEIYVE GKLVNLVIK