SYL_CAMLR
ID SYL_CAMLR Reviewed; 809 AA.
AC B9KCS8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, 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}; OrderedLocusNames=Cla_1045;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM64367.1; -; Genomic_DNA.
DR RefSeq; WP_012661750.1; NC_012039.1.
DR AlphaFoldDB; B9KCS8; -.
DR SMR; B9KCS8; -.
DR STRING; 306263.Cla_1045; -.
DR EnsemblBacteria; ACM64367; ACM64367; CLA_1045.
DR GeneID; 7410779; -.
DR KEGG; cla:CLA_1045; -.
DR PATRIC; fig|306263.5.peg.1029; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000007727; 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; 2.
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_1000199186"
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; 93357 MW; AE1DA80F77FDCD12 CRC64;
MAYEAGKIEK KWQKIWQEKE YFEPKDDFSL PKKYILSMFP YPSGRIHMGH VRNYSIGDAM
ARYYRKKGFN VLHPIGFDSF GMPAENAAIK HGIHPKKWTY ENIDYMQNEL ASLGFSFSKK
RMLATSDPLY TKFEQEFFIK MYEKGLIYTK EAEVNWCEND KTVLANEQVE DGKCWRCGHE
VIRKKMPGYY VKITAYADEL LQDLKKLEGK WPSQVLTMQE NWIGKSTGLS FDFDIEENNK
ISAKKINVFT TRAETIYGVS YIALAPDHEI VNELIDKKLL DQDVIAKIQN IQNQTPRQRQ
AAPKEGYFLN LYVIHPLSKE KIPLWVANFV LSDYGSGAVM SVPAHDERDY EFAKTYNLAI
KKVIYKDEND AQCYTLKEGV LTSSGEFDQL ECNDAREKIS LKIESLGIGK KVTNFKIRDW
GVSRQRYWGA PIPMIKCDSC GIVPQKIENL PITLPEDVVI NGEGNPLDKH ETWKECICPK
CGKKAQKESD TLDTFFESSW YFARFASDDK TWQEKAVDEK SVNYWMNVDE YIGGIEHAIL
HLLYARFFQK ALRDLGYLKD DEPFNRLLTQ GMVTKDGAKM SKSKGNVVDP DYIIEKYGAD
SARLFILFAA PPAKELEWND SALEGAFKFI NRLYEKAMSL ECGKLQEIDH QSLNKEEKYA
RLKVYEALKK SFEVYEESFA FNTLIAACME ALNALNAINH KEVSKEAFYI ILNILEPIIP
HVCFELSEYL FKCENFKVLK IKDEVFIKDS FNIAISVNGK KRAQIEINSE AKEDEILALA
KENVAKWLEG KTIVKEIYID KKLVNLVVK
