SYK_GEOSE
ID SYK_GEOSE Reviewed; 494 AA.
AC Q9RHV9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=10737207; DOI=10.1271/bbb.64.432;
RA Takita T., Shimizu N., Sukata T., Hashimoto S., Akita E., Yokota T.,
RA Esaki N., Soda K., Inouye K., Tonomura B.;
RT "Lysyl-tRNA synthetase of Bacillus stearothermophilus molecular cloning and
RT expression of the gene.";
RL Biosci. Biotechnol. Biochem. 64:432-437(2000).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AB012100; BAA88691.1; -; Genomic_DNA.
DR PIR; JC7205; JC7205.
DR PDB; 3A74; X-ray; 1.80 A; A/B/C/D=2-494.
DR PDB; 3E9H; X-ray; 2.10 A; A/B/C/D=2-494.
DR PDB; 3E9I; X-ray; 2.20 A; A/B/C/D=2-494.
DR PDBsum; 3A74; -.
DR PDBsum; 3E9H; -.
DR PDBsum; 3E9I; -.
DR AlphaFoldDB; Q9RHV9; -.
DR SMR; Q9RHV9; -.
DR BRENDA; 6.1.1.6; 623.
DR EvolutionaryTrace; Q9RHV9; -.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..494
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152599"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 8..22
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 59..72
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 127..138
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 170..191
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3A74"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 278..297
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 423..438
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:3A74"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3A74"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:3A74"
SQ SEQUENCE 494 AA; 57406 MW; 109D1A4FDD7F714C CRC64;
MSHEELNDQL RVRREKLKKI EELGVDPFGK RFERTHKAEE LFELYGDLSK EELEEQQIEV
AVAGRIMTKR GMGKAGFAHI 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
