ID A0A2S0URL9_9RHOB Unreviewed; 526 AA.
AC A0A2S0URL9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN ORFNames=HYN69_15550 {ECO:0000313|EMBL:AWB50443.1};
OS Gemmobacter aquarius.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=2169400 {ECO:0000313|EMBL:AWB50443.1, ECO:0000313|Proteomes:UP000244496};
RN [1] {ECO:0000313|EMBL:AWB50443.1, ECO:0000313|Proteomes:UP000244496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0069 {ECO:0000313|EMBL:AWB50443.1,
RC ECO:0000313|Proteomes:UP000244496};
RA Yi H., Baek M.-G.;
RT "Genome sequencing of Gemmobacter.";
RL Submitted (APR-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_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; CP028918; AWB50443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0URL9; -.
DR KEGG; geh:HYN69_15550; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000244496; 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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR002904; Lys-tRNA-ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00467; lysS_arch; 1.
DR PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00177};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00177}; Reference proteome {ECO:0000313|Proteomes:UP000244496}.
FT MOTIF 44..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 290..294
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 526 AA; 58998 MW; 9202D774DF00AE33 CRC64;
MSALRDAAMK SKAWPFEEAR AILKRYEKKA PEKGYVLFET GYGPSGLPHI GTFGEVARTT
MIRRAFEIVS DIPTRLICFS DDVDGMRKVP ENVPQQDMLR QHMQKPLTSV PDPYGEYDSF
GAHNNAMLRR FLDTFGFAYE FISATEFYKS GQFDDTLRLA AERYDAIMAI MLASLRDERQ
KTYSAFLPIH PVTGRVLYVP MKEVNAKDGT ITFDDEDGRE WTLPVTGGNV KLQWKPDFGA
RWAALGVDFE MYGKDHSTNT PIYDGICEVL GGRKPNHMTY ELFLDDQGQK ISKSKGNGLT
IDEWLTYAAT ESLSYFMYQK PKTAKRMHFD VIPRAVDEYH QQLRAYGAQD VDAQVNNPVW
HIHGGNPPAS KMVVPFSMLL NLASVAGAKD AKGLWGFIRR YAPDASPEGN PDLDAAAGFA
VRYFADKIAP TRTFRLPTDM ERAAMDDLRA RLAAWDGGLD DEALQSMVFA VGKEHGFEPL
RDWFKALYEV LLGASDGPRF GGFVALYGVD ETVALMDRAL RGELVA
//
