ID   SYK_XYLFA               Reviewed;         506 AA.
AC   Q9PEB6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAY-2019, entry version 119.
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=XF_1112;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A.,
RA   Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R.,
RA   Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A.,
RA   Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P.,
RA   Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C.,
RA   Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A.,
RA   Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L.,
RA   Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y.,
RA   Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B.,
RA   Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S.,
RA   Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A.,
RA   Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B.,
RA   Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M.,
RA   de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E.,
RA   da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr.,
RA   da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A.,
RA   de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H.,
RA   Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L.,
RA   Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
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;
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000305}.
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DR   EMBL; AE003849; AAF83922.1; -; Genomic_DNA.
DR   PIR; E82721; E82721.
DR   RefSeq; WP_010893629.1; NC_002488.3.
DR   SMR; Q9PEB6; -.
DR   STRING; 160492.XF_1112; -.
DR   PRIDE; Q9PEB6; -.
DR   EnsemblBacteria; AAF83922; AAF83922; XF_1112.
DR   GeneID; 1126652; -.
DR   KEGG; xfa:XF_1112; -.
DR   eggNOG; ENOG4105CRK; Bacteria.
DR   eggNOG; COG1190; LUCA.
DR   KO; K04567; -.
DR   OMA; EIFGEKC; -.
DR   Proteomes; UP000000812; 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   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; 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   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN         1    506       Lysine--tRNA ligase.
FT                                /FTId=PRO_0000152708.
FT   METAL       416    416       Magnesium 1. {ECO:0000250}.
FT   METAL       423    423       Magnesium 1. {ECO:0000250}.
FT   METAL       423    423       Magnesium 2. {ECO:0000250}.
SQ   SEQUENCE   506 AA;  57532 MW;  B194E13ED1ECC6D0 CRC64;
     MTEHLPTSQV SFDENALIAE RRAKLLALRA QGVAYPNDVK REHYAADVQV AFANVETWTA
     EALEASGDRV RMAGRLMAKR LMGKASFAQI QDESGRIQLL IQSNVLGEDS YAAFKVLDVG
     DIIAVEGGLT RTRTGELSVK VNVLRLLTKA LRPLPDKWHG LTDVEQRYRQ RYVDLIVTPE
     SREIFIKRSK IIRALRTWLD ARLFLEVETP MMHYIPGGAA AKPFVTYHNA LDLELYLRVA
     PELYLKRLVV GGLERVYEIN RNFRNEGVST RHNPEFTMLE LYEAYSTYHE VMDLAETMIR
     DTAQSVLGTT QVIWDGAQID LGPIFRRWRM DEAVCHHNPE ISVAECTDRD ALLLHCERLK
     IKVKSSYGWG RLLLSIFEAT VEHTLIQPTF ITDHPVEISP LARESDIEPG YTDRFELFIN
     GKEIANGFSE LNDPEEQAMR FQKQVEAKEG GDDEAMYYDA DYIRALEYGM APTGGLGIGV
     DRLVMLLTGS TSIRDVLLFP YMRPER
//