(data stored in ACNUC10821 zone)

SWISSPROT: SYK_LISMF

ID   SYK_LISMF               Reviewed;         498 AA.
AC   Q724I4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00252};
GN   OrderedLocusNames=LMOf2365_0240;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529,
CC         ChEBI:CHEBI:456215; EC=6.1.1.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00252};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00252};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00252};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00252}.
DR   EMBL; AE017262; AAT03027.1; -; Genomic_DNA.
DR   RefSeq; WP_003728446.1; NC_002973.6.
DR   SMR; Q724I4; -.
DR   PRIDE; Q724I4; -.
DR   EnsemblBacteria; AAT03027; AAT03027; LMOf2365_0240.
DR   KEGG; lmf:LMOf2365_0240; -.
DR   HOGENOM; HOG000236578; -.
DR   KO; K04567; -.
DR   OMA; EIFGEKC; -.
DR   BioCyc; LMON265669:G1G0V-241-MONOMER; -.
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   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
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   PIRSF; PIRSF039101; LysRS2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q724I4.
DR   SWISS-2DPAGE; Q724I4.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    498       Lysine--tRNA ligase.
FT                                /FTId=PRO_0000152643.
FT   METAL       408    408       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00252}.
FT   METAL       415    415       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00252}.
FT   METAL       415    415       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00252}.
SQ   SEQUENCE   498 AA;  57409 MW;  768A4FFA57D2A090 CRC64;
     MSNENHEELN DQLIVRREKV DTLREEGIDP FGEKFIRSIS PEEIETKFAD KSKEELEEAA
     IEVSVAGRIM TKRVKGKVGF THIQDRFHQL QIYIRKDAIG EDAYAVFKLA DLGDIIGIKG
     TIFRTNTGEL SVKATEFTLL SKSLRPLPDK YHGLKDVEQR YRQRYLDLIT NEESQNRFVM
     RSKILKYTRD YMDNQGFLEV ETPVLHTIAG GAAAKPFITH HNALDMELYL RIALELHLKR
     LIVGGMDKVY EIGRVFRNEG TSTRHNPEFT MLESYAAYED YEDVMDLVEG LVSTVCKQVN
     GTTEITYGEY NVDLTPNWRR IHMADAVKEY VGVDFWNVTS DEEARELAKK HNVPVTEHMT
     YGHILNEFFE TYVEEKLIQP TFVYGHPVEI SPLAKKNKED DRFTDRFELF IVGREHANAF
     SELNDPIDQR ERFEAQMKER EQGNDEAHGM DADFLEALEY GLPPTGGLGI GIDRLVMLLT
     DAPSIRDILL FPTMKHRD
//

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