ID A0A0G9MR51_9SPHN Unreviewed; 545 AA.
AC A0A0G9MR51;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:KLE33187.1};
GN Synonyms=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN ORFNames=AAW01_04240 {ECO:0000313|EMBL:KLE33187.1}, BMF35_a2271
GN {ECO:0000313|EMBL:APE29100.1};
OS Aurantiacibacter gangjinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE33187.1, ECO:0000313|Proteomes:UP000053070};
RN [1] {ECO:0000313|EMBL:KLE33187.1, ECO:0000313|Proteomes:UP000053070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K7-2 {ECO:0000313|EMBL:KLE33187.1,
RC ECO:0000313|Proteomes:UP000053070};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APE29100.1, ECO:0000313|Proteomes:UP000183202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE29100.1,
RC ECO:0000313|Proteomes:UP000183202};
RA Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT "Complete genome sequence of two-chromosomal Erythrobacter gangjinensis
RT CGMCC 1.15024T, isolated from seawater.";
RL Submitted (NOV-2016) 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; CP018097; APE29100.1; -; Genomic_DNA.
DR EMBL; LBHC01000001; KLE33187.1; -; Genomic_DNA.
DR RefSeq; WP_047006036.1; NZ_LBHC01000001.1.
DR AlphaFoldDB; A0A0G9MR51; -.
DR STRING; 502682.BMF35_a2271; -.
DR KEGG; egn:BMF35_a2271; -.
DR PATRIC; fig|502682.8.peg.864; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000053070; Unassembled WGS sequence.
DR Proteomes; UP000183202; Chromosome i.
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:UP000053070}.
FT MOTIF 46..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 298..302
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 545 AA; 60368 MW; 0816C115FDB56284 CRC64;
MFSTDLIAAA RSSKAWPFVE AQRLAKRFRD GKPGGEPVLF ETGYGPSGLP HIGTFQEVLR
TTLVRKAYEI VGAAEDGTPA PTRLVAFSDD MDGLRKVPDN LPNPAMLAKH LGKPLCQIPD
PFEKYESFAH HNNAMLRDFL DRFGFEYEFV AASDRYNSGA FDGALANVLR NYDSIMDIML
PTLREERRQT YSPVLPVSPT TGAVLQVPVE VVDADAGMVR FTDEDGSTVE QSVFGGQAKL
QWKVDWAMRW VDLGVDYEMY GKDLTDSGVQ SGRIAKVLGG RKPEGMIYEM FLDAAGEKIS
KSKGNGLSIE EWLTYGSQES LSHYIYANPK SAKQLHAGII PRAVDEYWQF RERIPEQELD
KQLGNPAWHL LRVEHGGDSQ PPQGAGDSLP VTYGLLLNLA SVLGTEASAD SLRDYVASYS
DDAAGNPHVE RLIETAIAYN RDFVAPTLNK RAPTDSEAGA LRELDAGLQL LDVNSTAEEL
QSLVYEIGKK EQFGFTNLRD WFRCLYETLL GSSQGPRMGS FIALYGIENT RSLIEEALNR
DRASR
//
