ID A0A1D9BAE0_9NEIS Unreviewed; 502 AA.
AC A0A1D9BAE0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=BJP62_02095 {ECO:0000313|EMBL:AOX99349.1};
OS Jeongeupia sp. USM3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Jeongeupia.
OX NCBI_TaxID=1906741 {ECO:0000313|EMBL:AOX99349.1, ECO:0000313|Proteomes:UP000176825};
RN [1] {ECO:0000313|EMBL:AOX99349.1, ECO:0000313|Proteomes:UP000176825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USM3 {ECO:0000313|EMBL:AOX99349.1,
RC ECO:0000313|Proteomes:UP000176825};
RA Kho H.P.;
RT "Jeongeupia sp. strain USM3 Genome sequencing and assembly.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOX99349.1, ECO:0000313|Proteomes:UP000176825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USM3 {ECO:0000313|EMBL:AOX99349.1,
RC ECO:0000313|Proteomes:UP000176825};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; CP017668; AOX99349.1; -; Genomic_DNA.
DR RefSeq; WP_070526015.1; NZ_CP017668.1.
DR AlphaFoldDB; A0A1D9BAE0; -.
DR STRING; 1906741.BJP62_02095; -.
DR KEGG; jeu:BJP62_02095; -.
DR OrthoDB; 9801152at2; -.
DR Proteomes; UP000176825; 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; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00499; lysS_bact; 1.
DR PANTHER; PTHR42918:SF9; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000313|EMBL:AOX99349.1};
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|HAMAP-Rule:MF_00252};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252}.
FT DOMAIN 184..496
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ SEQUENCE 502 AA; 57137 MW; CB2A2B5036CC2850 CRC64;
MSEQQEHVVQ QDENQIMAER RAKLGALRKQ GPAFPNDFRR ADVAGDLHAR FDGVEKEDLE
AQNVTVSVAG RMMLKRVMGK ASFATVQDVS GRIQFYISRD SVGEEVYAAF KTWDMGDILG
AVGTLMKTKT GELSVQVTEL RLLTKSLRPL PDKFHGLADQ EQKYRQRYVD LIVSDVSRDT
FIKRSRIVQK IREYMVNESY LEVETPMMHP IPGGATAKPF TTHHNALDMP LFLRVAPELY
LKRLVVGGME RVFEVNRNFR NEGMSTRHNP EFTMMEFYEA YADYQRMMDM TEGVIRYAAR
EVIGHTVIEY QGKPVDLSKP FARFTIAGAI RHYNPQYTDE QLHDRAWLKA ELARLGAKPV
LTDGIGGLQL SLFDETTEEK LWEPTFIVDY PAEVSPLARA NDTNPGITER FELFMVGREH
ANGYSELNDP EDQAARFQAQ VDLKDKGDDE AMHFDADYIR ALEYGLPPTG GCGIGIDRLV
MLLTDSASIR DVILFPQMRR ED
//
