ID   SYK_BRUSU               Reviewed;         551 AA.
AC   P59225; G0KDF7;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; Synonyms=lysK;
GN   OrderedLocusNames=BRA0790, BS1330_II0783;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR   EMBL; AE014292; AAN33969.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20245.1; -; Genomic_DNA.
DR   RefSeq; WP_006192135.1; NZ_KN046805.1.
DR   AlphaFoldDB; P59225; -.
DR   SMR; P59225; -.
DR   EnsemblBacteria; AEM20245; AEM20245; BS1330_II0783.
DR   GeneID; 45053807; -.
DR   KEGG; bms:BRA0790; -.
DR   KEGG; bsi:BS1330_II0783; -.
DR   PATRIC; fig|204722.22.peg.2212; -.
DR   HOGENOM; CLU_025562_2_0_5; -.
DR   OMA; DWPMRWA; -.
DR   PhylomeDB; P59225; -.
DR   Proteomes; UP000007104; Chromosome II.
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:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR37940; PTHR37940; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00467; lysS_arch; 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..551
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152739"
FT   MOTIF           54..62
FT                   /note="'HIGH' region"
FT   MOTIF           303..307
FT                   /note="'KMSKS' region"
FT   BINDING         306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   551 AA;  61668 MW;  5E9B3CAB71A0EB80 CRC64;
     MTSHRLPEIT LTPELTAAAA EAKAWPFEEA RKILKRYAKT GLPETVIFET GYGPSGLPHI
     GTFGEVARTS MVRHAFRILT QDKVKTRLIC FSDDLDGMRK VPDNVPDRAA LEPYLQMPLS
     SVPNPFGGDY KSFAKHNNAM LCRFLDTFGF DYEFASATEY YRSGRFDTVL LKAVERYDDI
     MKVMLPTLGE ERQATYSPFL PISPKSGRVL YVPMKKVDAK AGTITFDDED GEETTLSVTG
     GKVKLQWKPD FGMRWAALGV DFEMFGKDHQ TNAGIYDRIC EILGGRAPEH FVYELFLDQL
     GQKISKSKGN GISIDEWLAY APTESLALYN FQKPKTAKKL YFDVIPKTVD EYFTYLSAYA
     RQEWKDRLNN PVWHIHYGNP PKADLPVTFA LMLNLVSASN AESPAVLWGF ISRHVPGVTP
     ENNPELDALV GYAIRYFNDF VKPTKKFRAP DDVERAALEA LDAKLGELPA GTDGNVIQNA
     ILDVARAIER YQDHTKKSPE GGPGVSVSFF QMLYEVLIGQ ERGPRFGSFV ALYGIDETRA
     LIKKALAGEL A