ID   SYK_AZOPC               Reviewed;         500 AA.
AC   B6YRR7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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}; OrderedLocusNames=CFPG_626;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(2008).
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_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 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00252}.
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DR   EMBL; AP010656; BAG83889.1; -; Genomic_DNA.
DR   RefSeq; WP_012573649.1; NC_011565.1.
DR   AlphaFoldDB; B6YRR7; -.
DR   SMR; B6YRR7; -.
DR   STRING; 511995.CFPG_626; -.
DR   EnsemblBacteria; BAG83889; BAG83889; CFPG_626.
DR   KEGG; aps:CFPG_626; -.
DR   eggNOG; COG1190; Bacteria.
DR   HOGENOM; CLU_008255_6_2_10; -.
DR   OMA; EIFGEKC; -.
DR   OrthoDB; 63621at2; -.
DR   Proteomes; UP000000723; 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..500
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_1000125513"
FT   BINDING         407
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT   BINDING         414
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT   BINDING         414
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   500 AA;  58279 MW;  8D6958FFC10AAA81 CRC64;
     MSEQEIFRRK SLEELKSRGI DPYPADEYIV TDYSTEIKRG FREDSPRWEV SVAGRMMSRR
     IMGKVSFVEL QDSVGRIQLY IKCDSLCPNE NKDLYYIVFK KLLDIGDFIG IKGYVFCTQT
     GEISIHVNSL TLLSKSLRPL PIVKSKDGMT YDSYNDVELR YRQRYVDLIV NEGTKDIFLK
     RTKIFNSVRS FFNEKGYIEV DTPVLQSIPG GAAARPFVTH HNALDIPCYL RIANELYLKR
     LIVGGFEGVY EFSRNFRNEG IDKVHNPEFT VVEVYVSYKD YKWMMNFTEQ MLEHICIEIL
     GSTELKIGEY IINFKAPYRR ITMIDVIEEN TGVNIAGMNE NQLREVCRFL HIEEDKTMSS
     GKLIDEIFGK KCEWKYIQPT FIIDYPKEMS PLCKCHRQNA ELTERFELIV NGFELANAYS
     ELNDPIDQRK RFEDQLKLSK KGDNEAMFID QDFLRALEYG MPPTSGMGIG MDRLVMLLTK
     QTSIQEVLLF PHMRPEKLDY