ID   EPMA_BUCAP              Reviewed;         324 AA.
AC   Q9Z614;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=BUsg_561;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Clark M.A., Baumann P., Moran M.A.;
RT   "Buchnera plasmid-associated trpEG probably originated from a chromosomal
RT   location between hslU and fpr.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE013218; Type=Frameshift; Note=This may be a natural frameshift.; Evidence={ECO:0000305};
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DR   EMBL; AF108665; AAD19636.1; -; Genomic_DNA.
DR   EMBL; AE013218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q9Z614; -.
DR   SMR; Q9Z614; -.
DR   OMA; EWYRPGF; -.
DR   Proteomes; UP000000416; Chromosome.
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   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   5: Uncertain;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..324
FT                   /note="Elongation factor P--(R)-beta-lysine ligase"
FT                   /id="PRO_0000152717"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         99..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         243..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
SQ   SEQUENCE   324 AA;  38308 MW;  FF5458CAE0DE3612 CRC64;
     MKKKWKPSAS IKDLMKRSKI IADIRSFFLK KNIMEVETPI LSQSGVTDVN LMPFITNYFS
     FNDNIKKKNL WLITSPEYHM KRLLSAGSGS IYQICRSFRN QEFGQYHNPE FTMLEWYQLS
     CSMEKMIEEI DFFFQKILNF NKADKISYQE VFMKFLKIDP LSTSLSELFQ CYKKFNLKNL
     IYLENDLNQL IENIFTLQIQ PFLGKEKPLF VYHFPSEQAC LASINKKDSR VSERFEIFFK
     GIELGNGFHE LTDYFEQRKR FIKDNRKRCD MNLPEQKIDD YFLDAIHHGL PTCSGVAIGL
     DRLIMIALNK NSIDQVMSFS FERS