ID   SYL_CAMFF               Reviewed;         811 AA.
AC   A0RNX3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, 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=CFF8240_0731;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-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; CP000487; ABK82789.1; -; Genomic_DNA.
DR   RefSeq; WP_002849157.1; NC_008599.1.
DR   AlphaFoldDB; A0RNX3; -.
DR   SMR; A0RNX3; -.
DR   STRING; 360106.CFF8240_0731; -.
DR   EnsemblBacteria; ABK82789; ABK82789; CFF8240_0731.
DR   GeneID; 61064571; -.
DR   KEGG; cff:CFF8240_0731; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000760; 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.
FT   CHAIN           1..811
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009316"
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   811 AA;  93325 MW;  7A2CFDF0E6B32A25 CRC64;
     MEYNAKNIEY KWQQIWKKNG YSEPKDDYSL PKKYILSMFP YPSGRLHMGH VRNYSIGDAL
     SRYYRNRGYN VLQPIGFDSF GMPAENAAIK HKIHPKIWTY DNIDYMTKEL DALGFSFSKK
     RLFATSDPLY TRWEQEFFIR MYEKGLVYRK SAVVNWCEND QTVLANEQVE DGKCWRCGHE
     VIQKEMPGYY LKITDYANEL LECLKDLEGK WPNQVLTMQE NWIGKSYGLE FEFKFDSSSK
     ILLDGMDGFK VFTTRPDTIY GVSYAAIAPE HIVVKKLLEK NILDDATSAK LKFILNQSPK
     QRQSIDKDGV SLGLNVIHPL TNELIPVWCA NFVLAEYGGG AVMSVPAHDE RDFEFASKFN
     LNIKQIIKSD TLPYCEKSGV YINSELINGL AYEEAREKII SKFEKEGWGN RVTNYKLRDW
     GISRQRYWGA PIPMIHCKKC GVVPENISNL PVKLPDDVVI TGEGNPLDKH SEFKNCKCPK
     CGSQATRETD TMDTFFESSW YFARFASDEK TWEDVAFDKK SVDYWMSVDQ YIGGIEHAIL
     HLLYARFFQK ALRDLGYLRD CEPFDSLLTQ GMVLKDGSKM SKSKGNTVDP DDIINKFGAD
     TARLFILFAA PPQKELEWND SAVEGAFKFI NRLYDRSDNA YKTEILPQIN HSNLNKDEKY
     ARLKVYEALK KSTDVFENSF AFNTLIAACM EALNGLNAQN NKDIWTEGYF IILNLLEPII
     PHACHELSNE LFGLKNFTKL SLKDEVFVKD SLNLAITVNG KRRSEIEVSA FESDDKILEI
     AKQEVSKWIE GKEILKEIYV PNKLVNLVIK G