ID   SYL_CAMJE               Reviewed;         809 AA.
AC   Q9PNK3; Q0P9G3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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}; OrderedLocusNames=Cj1091;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35208.1; -; Genomic_DNA.
DR   PIR; F81312; F81312.
DR   RefSeq; WP_002852890.1; NC_002163.1.
DR   RefSeq; YP_002344484.1; NC_002163.1.
DR   AlphaFoldDB; Q9PNK3; -.
DR   SMR; Q9PNK3; -.
DR   STRING; 192222.Cj1091c; -.
DR   PaxDb; Q9PNK3; -.
DR   PRIDE; Q9PNK3; -.
DR   EnsemblBacteria; CAL35208; CAL35208; Cj1091c.
DR   GeneID; 905382; -.
DR   KEGG; cje:Cj1091c; -.
DR   PATRIC; fig|192222.6.peg.1073; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000799; 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; 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; 2.
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; Reference proteome.
FT   CHAIN           1..809
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151992"
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;  93431 MW;  D7300CDA3DEF8C39 CRC64;
     MAYEASLIEK KWQKIWDENE YFEPKDDLNL PKKYILSMFP YPSGRIHMGH VRNYTIGDAL
     ARYYRKIGFN VLHPIGFDSF GMPAENAAIK HKIHPKSWTY ENIAYMKKEL FSLGFSFSKK
     RMLATSDPLY TKFEQEFFIK MFEKGLIYTK EANVNWCEQD QTVLANEQVE DGKCWRCGHE
     VVQKKMPGYY VKITAYAEEL LKDLEELKDK WPNQVLTMQE NWIGKSEGLE FSLNLDEESK
     QKTKESSLEV FTTRADTIYG VSYIALAPEH KIVQNLLSQN LLNQDVLNKI KVIQNQSPRE
     RQSSEKEGYF LGIYAIHPLS GEKIPLWVAN FVLADYGSGA VMAVPAHDER DFEFATKYNL
     AIKQVIQTQE NLPYMQKLGK LINSQEFDNL 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