ID   SYK_ROSDO               Reviewed;         527 AA.
AC   Q16AV0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=RD1_1246;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG30893.1; -; Genomic_DNA.
DR   RefSeq; WP_011567513.1; NZ_FOOO01000008.1.
DR   AlphaFoldDB; Q16AV0; -.
DR   SMR; Q16AV0; -.
DR   STRING; 375451.RD1_1246; -.
DR   EnsemblBacteria; ABG30893; ABG30893; RD1_1246.
DR   KEGG; rde:RD1_1246; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_2_0_5; -.
DR   OMA; DWPMRWA; -.
DR   OrthoDB; 256927at2; -.
DR   Proteomes; UP000007029; 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: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; -; 2.
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; Reference proteome.
FT   CHAIN           1..527
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_1000040354"
FT   MOTIF           44..52
FT                   /note="'HIGH' region"
FT   MOTIF           290..294
FT                   /note="'KMSKS' region"
FT   BINDING         293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   527 AA;  59384 MW;  23D33C5964D04CA1 CRC64;
     MSDTRTAAMT SKAWPFEEAR RVLKRYEKNP PEKGYVLFET GYGPSGLPHI GTFGEVARTS
     MVMRAFQEIS DIPTRLICFS DDLDGMRKVP GNVPNPDALT EHLQRPLTSV PDPFGTHASF
     GAHNNAMLRR FLDTFGFEYE FISATEFYNT GQFDEILLRA AAKYDEIMAV MLKSLREERR
     QTYSIFLPIH PESGRVMYVP MKEVNAQAGT ITFDSEDGEE MTLPVTGGAV KLQWKPDFGA
     RWAALGVDFE MYGKDHSTNT PIYDKICRIL GQRPPEHFTY ELFLDENGQK ISKSSGNGVS
     IDEWLTYAST ESLSYFMYQK PKTAKRMYFD VIPKAVDEYH QQLRAYAGQD TAQRLNNPVW
     HIHGGDVPAS NMLVPFSMLL NLASVSSAED KSQLWGFIQR YAPESNPENN PDMDAAADFA
     VRYFNDFVKP KKVYRAASDL EREALEDLRD QLKAYDGPVD DEALQSIVYA CGRERFDPLR
     GWFTALYEVL LGASQGPRFG GFIALYGVQE TVALIDAALA GELLSDD