SYK_CAMJE
ID SYK_CAMJE Reviewed; 501 AA.
AC P41258; O68607; Q0PBA9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=Cj0401;
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 [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=1732205; DOI=10.1128/jb.174.3.695-701.1992;
RA Chan V.L., Bingham H.L.;
RT "Lysyl-tRNA synthetase gene of Campylobacter jejuni.";
RL J. Bacteriol. 174:695-701(1992).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-355.
RC STRAIN=ATCC 700819 / NCTC 11168;
RA van Vliet A.H.M., Wooldridge K.G., Ketley J.M.;
RT "Characterisation of a Campylobacter jejuni fur mutant.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M63448; AAA23029.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34551.1; -; Genomic_DNA.
DR EMBL; AF052056; AAC64260.1; -; Genomic_DNA.
DR PIR; A42609; A42609.
DR PIR; G81383; G81383.
DR RefSeq; WP_002858694.1; NC_002163.1.
DR RefSeq; YP_002343838.1; NC_002163.1.
DR AlphaFoldDB; P41258; -.
DR SMR; P41258; -.
DR IntAct; P41258; 54.
DR STRING; 192222.Cj0401; -.
DR PaxDb; P41258; -.
DR PRIDE; P41258; -.
DR EnsemblBacteria; CAL34551; CAL34551; Cj0401.
DR GeneID; 904725; -.
DR KEGG; cje:Cj0401; -.
DR PATRIC; fig|192222.6.peg.392; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_7; -.
DR OMA; EIFGEKC; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00775; LysRS_core; 1.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..501
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152608"
FT BINDING 404
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="N -> K (in Ref. 1; AAA23029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57846 MW; C8AA3D664A321728 CRC64;
MFDNILEQQR IEKAKELKNL GINPYPHFLE KEMSLKTFKD KFSYILEQVE KRDESVNAVV
AGRLKLLRIA GKSIFANIED EDTNLQIYFS KDSVGEELYT ILKKNLEVGD IVLVKGFPFV
TKTGEFSLHA SEVKLATKAI VPLPEKYHGL TDIEQRYRKR YVDMIMNVEV RKDFLVRSKV
VSLIRHFFEN KGFLEVETPM MHPIAGGANA KPFVTFHNSL GVERFLRIAP ELYLKRLIVG
GFEAVFEINR CFRNEGMDLT HNPEFTTIEF YWAYHNYKDL MDLTEELFAL LLDKLNLGKT
IEFDGKMINF SKPFERITYK DALCKYGGLD RDLIEDKEKI LTKLKADGFE ANEKLELGHL
QAELFDNYVE EKLINPTFVI DFPISISPLS RRSDEDSQIA ERFELFICGR ELANGFNELN
DPLDQYERFL KQIEAKNAGD EEACEMDEDF VNALGYGMPP TAGQGIGIDR LVMLLTNKKS
IRDVILFPAM RPLKSELKEK E
