ID A0A0P0P3N9_9CAUL Unreviewed; 551 AA.
AC A0A0P0P3N9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=lysK {ECO:0000313|EMBL:ALL14879.1};
GN Synonyms=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN ORFNames=AQ619_16740 {ECO:0000313|EMBL:ALL14879.1};
OS Caulobacter henricii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL14879.1, ECO:0000313|Proteomes:UP000056905};
RN [1] {ECO:0000313|EMBL:ALL14879.1, ECO:0000313|Proteomes:UP000056905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:ALL14879.1,
RC ECO:0000313|Proteomes:UP000056905};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013002; ALL14879.1; -; Genomic_DNA.
DR RefSeq; WP_062150314.1; NZ_CP013002.1.
DR AlphaFoldDB; A0A0P0P3N9; -.
DR STRING; 69395.AQ619_16740; -.
DR KEGG; chq:AQ619_16740; -.
DR eggNOG; COG1384; Bacteria.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000056905; 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; 1.
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:UP000056905}.
FT MOTIF 71..79
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 551 AA; 61425 MW; E2D7B727A475DA72 CRC64;
MFEGLSPLAR DARAWPFEQA RALLARTLRL RLSDAERDLA STLIHAGKTD EAVATLEALR
KPVVLETGYG PSGLPHMGTF GEVARTTMVR AAFRALTDDK IPTRLISFSD DMDGLRKIPP
NVPNGEVMIP DLDKPLTVVR DPYGEHESFG HHNNARLRTF LDGFGFDYEF VSSTDCYRGG
RFDETLLLAL ERFDAIQKIM LPSLGEERRA TYSPFLPISP KTGKVLQVPT LERNVAKGTI
VFRDEDGELT EVPVTGGGVK MQWRPDWAMR WTALGVDYEM SGKDLIDSVR LSNQVCKVLG
GSPPEGFHYE LFMDENNLKI SKTKGNGLTM DEWLRYGAPE SLAYYMFQSP KSAKKLYFDV
IPKATDEYLQ QLDAFQKQEP AKQIDNPAWH VHSGKPPEQG SPVSFSLMLN LVSAADASTK
DILWGFLGRY VDGATPESQP LLDRLAGYAI NYYEDFVKPS KTFRAPTDVE RAAIVDLRAR
LAALPEGCQD AELIQNEVFA VGKDHAFDPL RAWFQALYEV LLGQSQGPRF GSFAAIFGLD
RTIALIDEKL G
//
