ID EPMAH_AQUAE Reviewed; 293 AA.
AC O66963;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Elongation factor P--(R)-beta-lysine ligase homolog;
DE Short=EF-P--(R)-beta-lysine ligase homolog;
GN Name=genX; OrderedLocusNames=aq_763;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC EpmA subfamily. {ECO:0000305}.
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DR EMBL; AE000657; AAC06920.1; -; Genomic_DNA.
DR PIR; H70366; H70366.
DR RefSeq; NP_213524.1; NC_000918.1.
DR RefSeq; WP_010880462.1; NC_000918.1.
DR AlphaFoldDB; O66963; -.
DR SMR; O66963; -.
DR STRING; 224324.aq_763; -.
DR EnsemblBacteria; AAC06920; AAC06920; aq_763.
DR KEGG; aae:aq_763; -.
DR PATRIC; fig|224324.8.peg.607; -.
DR eggNOG; COG2269; Bacteria.
DR HOGENOM; CLU_008255_1_0_0; -.
DR InParanoid; O66963; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IBA:GO_Central.
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; IPR004525; EpmA.
DR NCBIfam; TIGR00462; genX; 1.
DR PANTHER; PTHR42918:SF6; ELONGATION FACTOR P--(R)-BETA-LYSINE LIGASE; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..293
FT /note="Elongation factor P--(R)-beta-lysine ligase homolog"
FT /id="PRO_0000152715"
FT BINDING 86..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 223..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 35013 MW; B8B38B08BDD0EB9B CRC64;
MDLLDAWDYF INEVRKFFKE KGYTEVSTPL LLDFPNLDSN VEPVKVEVLE RGENKVKWLH
TSPEYSMKKL LSRYKRDIFQ ITKVFRNNEW GRLHRIEFHM LEWYAVGCDY LYLIEELKQL
LNKLFGFKEF EVITVEEAFK RHFGEGIPQE ESSMKELLER KGIDFSEDED WETLFYRAFI
EVERHLGFNR PTFLINFPER LCALAKVRNG YAERFELFIK GIELANGWTE ETNPEEVRKR
LEREAKKRNL PLDEDFIKAH EDMPECAGCS LGIDRLFSLF LGKEELVSEF FRA
//
