ID A4CJH6_ROBBH Unreviewed; 563 AA.
AC A4CJH6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252};
GN OrderedLocusNames=RB2501_09280 {ECO:0000313|EMBL:EAR17084.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR17084.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR17084.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
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_00252, ECO:0000256|RuleBase:RU000336};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00252,
CC ECO:0000256|RuleBase:RU000336};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252,
CC ECO:0000256|RuleBase:RU000336};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00252}.
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DR EMBL; CP001712; EAR17084.1; -; Genomic_DNA.
DR RefSeq; WP_015753840.1; NC_013222.1.
DR AlphaFoldDB; A4CJH6; -.
DR STRING; 313596.RB2501_09280; -.
DR KEGG; rbi:RB2501_09280; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_2_10; -.
DR OMA; EIFGEKC; -.
DR OrthoDB; 9801152at2; -.
DR Proteomes; UP000009049; 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: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; Nucleic acid-binding proteins; 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; 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 NCBIfam; TIGR00499; lysS_bact; 1.
DR PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00252};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00252}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00252};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252};
KW Reference proteome {ECO:0000313|Proteomes:UP000009049}.
FT DOMAIN 181..491
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 414
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 414
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ SEQUENCE 563 AA; 64191 MW; 3F91435076E5C8FD CRC64;
MQLSEQEIIR REKLRQLREL GIDPYPAEKY PVDTLSSSVR ENYEEGKHVV MAGRLMSRRI
QGKASFAELQ DSAGRIQLYF NRDEICEGED KSAYNDIYKK LLDIGDIIGI EGELFKTQVG
EKTVRVKRFT LLSKALRPLP LPKKDAEGKV FDEFNDPEQR YRMRYVDLVV NPNVRETFVK
RTKITNSIRR FFNEKGYLEV ETPILQPIPG GAAARPFQTH HNALGIPLYL RIANELYLKR
LIVGGFDGVY EFAKDFRNEG MDRTHNPEFT VMELYVAYKD YNWMMETTEQ LLERVAREAN
GSTRVSAGGE TIDFKAPYPR VPILDAIREH TGIDVDGMDE AALRDAAAGL GIEVDESMGV
GKLIDEIFGE CCEHHYVQPT FIIDYPKEMS PLTKAHRSKP GLTERFELLV NGKEIANAYS
ELNDPIDQRE RFEEQLKLSE KGDDEAMFID RDFLRALEFG MPPTSGIGIG IDRLVMLLTD
NSSIQEVLFF PQMKPEKKPL ELNDEEKAIV NILRPAAEMD LGILKEKAGL SNKKWDKATK
SLAKKGLFEV SKTEDGLLAR FKA
//