ID A0A0T6BS67_9BACI Unreviewed; 499 AA.
AC A0A0T6BS67;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ATH94015.1};
GN ORFNames=AB447_215155 {ECO:0000313|EMBL:KRT94493.1}, COP00_16440
GN {ECO:0000313|EMBL:ATH94015.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:KRT94493.1, ECO:0000313|Proteomes:UP000036168};
RN [1] {ECO:0000313|EMBL:KRT94493.1, ECO:0000313|Proteomes:UP000036168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT94493.1,
RC ECO:0000313|Proteomes:UP000036168};
RX PubMed=26297378; DOI=10.1099/ijsem.0.000462;
RA Kim S.J., Dunlap C.A., Kwon S.W., Rooney A.P.;
RT "Bacillus glycinifermentans sp. nov., isolated from fermented soybean
RT paste.";
RL Int. J. Syst. Evol. Microbiol. 65:3586-3590(2015).
RN [2] {ECO:0000313|EMBL:KRT94493.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT94493.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATH94015.1, ECO:0000313|Proteomes:UP000218414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBN06P03352 {ECO:0000313|EMBL:ATH94015.1,
RC ECO:0000313|Proteomes:UP000218414};
RA Yu W.-S., Do H.-N., Cheong H.-M., Hwang K.-J.;
RT "Whole genome sequencing of Bacillus glycinfermentans NCCP 15922.";
RL Submitted (SEP-2017) 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; CP023481; ATH94015.1; -; Genomic_DNA.
DR EMBL; LECW02000011; KRT94493.1; -; Genomic_DNA.
DR RefSeq; WP_048355685.1; NZ_LECW02000011.1.
DR AlphaFoldDB; A0A0T6BS67; -.
DR STRING; 1664069.BGLY_0090; -.
DR OrthoDB; 9801152at2; -.
DR Proteomes; UP000036168; Unassembled WGS sequence.
DR Proteomes; UP000218414; 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:0016740; F:transferase activity; IEA:UniProt.
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; 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 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 PIRSF; PIRSF039101; LysRS2; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00252};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000313|EMBL:KRT94493.1};
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 183..494
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ SEQUENCE 499 AA; 57560 MW; 904B5EC3E0EC3032 CRC64;
MSHEEHNHEE LNDQLQVRRE KMSQLRESGK DPFGQRFDRS HQSGELIDLY NGFSKEELEE
KAIEVTIAGR MMTKRGKGKA GFAHIQDLQG QIQIYVRKDS VGEERYELFK SSDLGDIVGV
TGVMFKTNVG ELSVKATSFD LLTKALRPLP DKYHGLKDIE QRYRQRYLDL IVNPDSKKTF
IARSKIIQSM RRYLDSHGYL EVETPMMHSI PGGASARPFI THHNALDMPL YMRIAIELHL
KRLIVGGLEK VYEIGRVFRN EGVSTRHNPE FTMIELYEAY ADYKDIMRLT ENLIAHIAEE
VLGTTTVQYG EHEVDLKPEW KRLHMVDAVK ELTGIDFWKE VSLAEARAYA KEHGVEISEN
MSVGHIINEF FEQKVEETLI QPTFIYGHPV EISPLAKKNP EDPRFTDRFE LFIVGREHAN
AFTELNDPID QKERFEAQLK EREEGNDEAH MMDEDFVEAL EYGMPPTGGL GIGIDRLIML
LTNSPSIRDV LLFPQMRHR
//
