ID SYL_CAMC1 Reviewed; 821 AA.
AC A7ZE39;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Ccon26_11910; ORFNames=CCC13826_0074;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-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; CP000792; EAT97782.1; -; Genomic_DNA.
DR RefSeq; WP_012139968.1; NC_009802.2.
DR AlphaFoldDB; A7ZE39; -.
DR SMR; A7ZE39; -.
DR STRING; 360104.CCC13826_0074; -.
DR KEGG; cco:CCC13826_0074; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000001121; 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..821
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334738"
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; 94106 MW; E00E273EF5B2431C CRC64;
MAEKRKYEPL KIEKKWQEIW DKNEEFEPKD DLSLPKKYIL SMFPYPSGRI HMGHVRNYSI
GDALARSYRK SGYNVLHPIG FDSFGMPAEN AAIKHKIHPK IWTYENIDYM KKELASLGFS
FSKKRILATS DPLYTKWEQS FFIKMFEKGL VYRKNAIVNW CEYDQTVLAN EQVEDGKCWR
CGNDVVQKEL PGYYFNITKY ASELLDDLKL LEGKWPNQVI TMQENWIGRS YGLEFKFSLD
EASKETLGGK FDGFEVFTTR PDTIYGVSYT ALAPEHPIVK ALLESDKFDE NKKAKIKAIL
NQSPRERQAS DKDGEFLGIY VVHPLTNEKI PVWVANFILA DYGSGAIMAV PAHDQRDFEF
ASKFNLPIKP VVKPLEGESE GSKAYSEYGV AINSELINGL SSEDAKSFII EKFEKDGLGK
RITNYKLRDW GISRQRYWGA PIPVVHCKCC GVVPEKEENL PIALPEDVEI TGEGNPLDKH
PTWKFTKCPK CGKDAIRETD TMDTFVESSW YFARFASDEK TWEQKALDEK SVNYWMNVDQ
YIGGIEHAIL HLLYARFFQK VLRDLGYLRD DEPFENLLTQ GMVLKDGKKM SKSKGNVVDP
DDIINRYGAD TARLFILFAA PPQKELEWND SAVEGAFRFL NRLWEKSQTI KKIDKLPEID
HESLNKDEKF ARLKIYEALK KSTEVFGDTF AFNTLIAACM EALNAINAQD NDDVNAEGFF
IILNLLEPIV PHIANELSEE LFGRKNFTKI AVKEEVFVKD SIALAVTVNG KKRAEFEVTA
SENESEILKQ AKQNVAKWLE GKEILKEIYI KGKLVNFVIK G
//
