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   03-AUG-2022, entry version 112.
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; 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}.
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; 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   OMA; EWYRPGF; -.
DR   OrthoDB; 63621at2; -.
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   Gene3D; 3.30.930.10; -; 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; IPR004525; EpmA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00462; genX; 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