ID   SYL_CAMC5               Reviewed;         821 AA.
AC   A7GZ81;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=Ccur92_12190; ORFNames=CCV52592_0710;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
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   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
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; CP000767; EAU00405.1; -; Genomic_DNA.
DR   RefSeq; WP_011992459.1; NC_009715.2.
DR   AlphaFoldDB; A7GZ81; -.
DR   SMR; A7GZ81; -.
DR   STRING; 360105.CCV52592_0710; -.
DR   KEGG; ccv:CCV52592_0710; -.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006380; 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; Reference proteome.
FT   CHAIN           1..821
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334739"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           589..593
FT                   /note="'KMSKS' region"
FT   BINDING         592
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   821 AA;  93990 MW;  66AF609B342A47A3 CRC64;
     MAQNSKYEAA KIEKKWQEIW HKNGEFEPKD DYTLPKKYIL SMFPYPSGRI HMGHVRNYSI
     GDALARYYRK NCFNVLHPIG FDSFGMPAEN AAIKHKIHPK KWTYENIDYM KKELSSLGFS
     FSDRRMLATS DPLYTKWEQS FFIKMFEKGL VYRKSAIVNW CEHDQTVLAN EQVEDGCCWR
     CGNEVVQREF PGYYFKITQY AEELLNDLKT LEGKWPNQVI AMQENWIGKS SGLEFKFYLD
     DASSRALGGK FDGFEVFTTR PDTIYGVSYV ALAPEHKVVR ALLSSEILDD TKKAKIKSIL
     NQSPRERQAS DKDGVFLDIY MLHPLTNEPV PVWVANFILA DYGSGAIMAV PAHDQRDYEF
     ASKFGLPIKQ VVMPKEGKFD TSKANAEYGI SINSPLINGL ETKQAKQAII EKFEKDGLGK
     RITNYKLRDW GISRQRYWGA PIPIVHCPNC GVVPENEQNL PIALPDDVVI TGEGNPLDKH
     PTWKYTKCPK CGHDAVRETD TMDTFVESSW YFARFASDEK TWQQTAFDKK SVDYWMSVDQ
     YIGGIEHAIL HLLYARFFQK VLRDLGYLRD DEPFSNLLTQ GMVLKDGKKM SKSKGNVVDP
     DDIINRYGAD TARLFILFAA PPQKELEWND SAVEGAYRFL NRLWDKAKTI KKSEILPAIE
     HANLNKDEKY ARMKVYEALK KSNEVFNETF AFNTLIAACM EALNALNAQD NDDVNTEGFF
     IILNLLEPIV PHIANELSEE LFRRKNFTKL EILEEVFVKD TINLAVTVNG KKRAEFEISA
     DASEADVLQT AKASVAKWIE GKEIIKEIYI KGKLVNLVVK G
//