SYK_BACTN
ID SYK_BACTN Reviewed; 576 AA.
AC Q8A5W4;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BT_2122;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO77229.1; -; Genomic_DNA.
DR RefSeq; NP_811035.1; NC_004663.1.
DR RefSeq; WP_008759776.1; NZ_UYXG01000026.1.
DR AlphaFoldDB; Q8A5W4; -.
DR SMR; Q8A5W4; -.
DR STRING; 226186.BT_2122; -.
DR PaxDb; Q8A5W4; -.
DR PRIDE; Q8A5W4; -.
DR EnsemblBacteria; AAO77229; AAO77229; BT_2122.
DR GeneID; 60928110; -.
DR KEGG; bth:BT_2122; -.
DR PATRIC; fig|226186.12.peg.2184; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_10; -.
DR InParanoid; Q8A5W4; -.
DR OMA; EIFGEKC; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IBA:GO_Central.
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; IPR025567; DUF4332.
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; PF14229; DUF4332; 1.
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..576
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152601"
FT BINDING 413
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
SQ SEQUENCE 576 AA; 65965 MW; 2BC8092D3A772242 CRC64;
MNILELSEQE IIRRNSLNEL RAMGIDPYPA AEYVTNAFST DIKAEFKDED EPRQVSVAGR
IMSRRVMGKA SFIELQDSKG RIQVYITRDD ICPGEDKELY NSVFKRLLDL GDFVGIEGFV
FRTQMGEISI HAKKLTVLAK SIKPLPIVKY KDGVAYDSFE DPELRYRQRY VDLVVNEGIK
ETFEKRATVV RTLRNALDEA GYTEVETPIL QSIAGGASAR PFITHHNSLD IDLYLRIATE
LYLKRLIVGG FEGVYEIGKN FRNEGMDRTH NPEFTCMELY VQYKDYNWMM SFTEKLLERI
CIAVNGSTET VVDGKTISFK APYRRLPILD AIKEKTGYDL NGKSEEEIRQ ICKELKMEEI
DDTMGKGKLI DEIFGEFCEG SYIQPTFITD YPVEMSPLTK MHRSKPGLTE RFELMVNGKE
LANAYSELND PLDQEERFKE QMRLADKGDD EAMIIDQDFL RALQYGMPPT SGIGIGIDRL
VMLMTGQTTI QEVLFFPQMR PEKVIKKDPA AKYMELGIAE DWVPVIQKAG YNTVADMQDV
NPQKLHQDIC GINKKYKLEL TNPSVNDVTE WINKLK
