ID A0A291GCA3_9RHOB Unreviewed; 547 AA.
AC A0A291GCA3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=CEW89_08935 {ECO:0000313|EMBL:ATG47684.1};
OS Celeribacter ethanolicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG47684.1, ECO:0000313|Proteomes:UP000217935};
RN [1] {ECO:0000313|EMBL:ATG47684.1, ECO:0000313|Proteomes:UP000217935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSPH2 {ECO:0000313|EMBL:ATG47684.1,
RC ECO:0000313|Proteomes:UP000217935};
RA Woo J.-H., Kim H.-S.;
RT "Celeribacter sp. TSPH2 complete genome sequence.";
RL Submitted (JUN-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_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; CP022196; ATG47684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GCA3; -.
DR STRING; 1758178.GCA_001550095_01304; -.
DR KEGG; ceh:CEW89_08935; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000217935; 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:UP000217935}.
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 547 AA; 61863 MW; AD230D872D2847B8 CRC64;
MTDLRDAGMS SKAWPFEEAR TVLKRYEASK DKKGYVLFET GYGPSGLPHI GTFGEVLRTT
MIRRAFEVIS DVPTRLICFS DDMDGMRKVP SNVPNQELLH ENLHKPLTSV PDPFEEFESF
GHHNNAMLRR FLDTFGFEYE FYSATEFYKT GQFDEILKRA VEKYDDVMKV MLKSLREERQ
QTYSIFLPIH PETGRVLYVP MKSVNKDDYT ITFDDEDGRE WTLPVTGGAV KLQWKPDFGA
RWAALDVDFE MYGKDHSTNT PIYDRICEIL GGKKPEHFTY ELFLDANGEK ISKSKGNGLS
IDEWLTYAST ESLAYFMYQK PKTAKRLHFD VIPRMMDEYH QQLRAYPGQD AAQKAANPVF
HIHGADVPLS DMVVPFSMLL NLASVAGAEE KEQLWGFIQR YAPEASPEAN PQLDAAAGYA
VRYYNDFVKP EKVFRAPTAQ ERAAMEDLKA AFGSSEVALA AIARKNADMG NDEALPEADF
ADGDFLQSIV FAVGKNHGFE NLRDWFKALY EVLLGQSQGP RFGSFAALYG VTETIALIDK
GLSGELS
//
