ID   EPMA_VIBVY              Reviewed;         323 AA.
AC   Q7MGX9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Elongation factor P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174};
DE            Short=EF-P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174};
DE            EC=6.3.1.- {ECO:0000255|HAMAP-Rule:MF_00174};
DE   AltName: Full=EF-P post-translational modification enzyme A {ECO:0000255|HAMAP-Rule:MF_00174};
DE   AltName: Full=EF-P-lysine lysyltransferase {ECO:0000255|HAMAP-Rule:MF_00174};
GN   Name=epmA {ECO:0000255|HAMAP-Rule:MF_00174}; Synonyms=yjeA;
GN   OrderedLocusNames=VV3096;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: With EpmB is involved in the beta-lysylation step of the
CC       post-translational modification of translation elongation factor P (EF-
CC       P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced
CC       by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is
CC       then transferred to the epsilon-amino group of a conserved specific
CC       lysine residue in EF-P. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       EpmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00174}.
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DR   EMBL; BA000037; BAC95859.1; -; Genomic_DNA.
DR   RefSeq; WP_011079255.1; NC_005139.1.
DR   AlphaFoldDB; Q7MGX9; -.
DR   SMR; Q7MGX9; -.
DR   STRING; 672.VV93_v1c28190; -.
DR   PRIDE; Q7MGX9; -.
DR   EnsemblBacteria; BAC95859; BAC95859; BAC95859.
DR   KEGG; vvy:VV3096; -.
DR   PATRIC; fig|196600.6.peg.3070; -.
DR   eggNOG; COG2269; Bacteria.
DR   HOGENOM; CLU_008255_1_1_6; -.
DR   OMA; EWYRPGF; -.
DR   OrthoDB; 63621at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0071915; P:protein-lysine lysylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00174; EF_P_modif_A; 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   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
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..323
FT                   /note="Elongation factor P--(R)-beta-lysine ligase"
FT                   /id="PRO_0000152733"
FT   BINDING         74..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         98..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         242..243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
SQ   SEQUENCE   323 AA;  36147 MW;  ABD9CC984E9F7E5C CRC64;
     MQADWKPTAS IEQLRQRAVL IANIRQFFAQ RGVLEVDTPA MSHATVTDIH LHTFQTEFVG
     PGYAQGRHLH LMTSPEFHMK RLLAAGSGCI YQMAKAFRNE ENGRHHNPEF TMLEWYRVGF
     DHHQLMDEMD DLLQLILKCG TAERMTYQQA FLTVLGVCPL EGSMAELKSV AARLGLSDIA
     EPEEDRDTLL QLLFSIGVEA KIGQQVPAFV YDFPASQAAL AKINPNDPRV ADRFEVYFKG
     IELANGFHEL DNPQEQLTRF EQDNAKRIDM GLTPQPIDYH LIAALESGLP ACAGVALGVD
     RLIMLSLGCT HIDEITAFPF PIA