ID A0A377GZS9_9BACL Unreviewed; 494 AA. AC A0A377GZS9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 25-MAY-2022, entry version 16. DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252}; DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252}; DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252}; DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252}; GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252, GN ECO:0000313|EMBL:STO35825.1}; GN ORFNames=NCTC11526_02765 {ECO:0000313|EMBL:STO35825.1}; OS [Flavobacterium] thermophilum. OC Bacteria; Firmicutes; Bacilli; Bacillales. OX NCBI_TaxID=1414643 {ECO:0000313|EMBL:STO35825.1, ECO:0000313|Proteomes:UP000255043}; RN [1] {ECO:0000313|EMBL:STO35825.1, ECO:0000313|Proteomes:UP000255043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC11526 {ECO:0000313|EMBL:STO35825.1, RC ECO:0000313|Proteomes:UP000255043}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP- CC Rule:MF_00252, ECO:0000256|RuleBase:RU000336}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00252, CC ECO:0000256|RuleBase:RU000336}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252, CC ECO:0000256|RuleBase:RU000336}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00252}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; UGGS01000002; STO35825.1; -; Genomic_DNA. DR EnsemblBacteria; STO35825; STO35825; NCTC11526_02765. DR Proteomes; UP000255043; Unassembled WGS sequence. 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; IPR034762; Lys-tRNA-ligase_II_bac/euk. 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 PIRSF; PIRSF039101; LysRS2; 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 {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00252}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00252}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252, KW ECO:0000256|RuleBase:RU000336}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00252}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00252}. FT DOMAIN 178..489 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" FT COILED 3..23 FT /evidence="ECO:0000256|SAM:Coils" FT METAL 405 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" FT METAL 412 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" FT METAL 412 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252" SQ SEQUENCE 494 AA; 57402 MW; 9F90D616FCC9F663 CRC64; MSHEELNDQL RVRREKLKKI EELGVDPFGK RFERTHKAQE LFELYGDLSK EELEEQQIEV AVAGRIMTKR GKGKAGFAHI QDVTGQIQIY VRQDDVGEQQ YELFKISDLG DIVGVRGTMF KTKVGELSIK VSSYEFLTKA LRPLPEKYHG LKDIEQRYRQ RYLDLIMNPE SKKTFITRSL IIQSMRRYLD SHGYLEVETP MMHAVAGGAA ARPFITHHNA LDMTLYMRIA IELHLKRLIV GGLEKVYEIG RVFRNEGIST RHNPEFTMLE LYEAYADFRD IMKLTENLIA HIATEVLGTT KIQYGEHLVD LTPEWRRLHM VDAIKEYVGV DFWRQMSDEE ARELAKEHGV EVAPHMTFGH IVNEFFEQKV EDKLIQPTFI YGHPVEISPL AKKNPDDPRF TDRFELFIVG REHANAFTEL NDPIDQRQRF EEQLKEREQG NDEAHEMDED FLEALEYGMP PTGGLGIGVD RLVMLLTNSP SIRDVLLFPQ MRHK //