ID   EPMA_SALDC              Reviewed;         325 AA.
AC   B5FRL4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   02-SEP-2026, entry version 79.
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=6.3.2.- {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=SeD_A4741;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-
CC       lysine produced by EpmB, forming a lysyl-adenylate, from which the
CC       beta-lysyl moiety is then transferred to the epsilon-amino group of EF-
CC       P 'Lys-34'. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-beta-lysine + L-lysyl-[protein] + ATP = N(6)-((3R)-3,6-
CC         diaminohexanoyl)-L-lysyl-[protein] + AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:83435, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:20131,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:84138, ChEBI:CHEBI:156053,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_00174};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83436;
CC         Evidence={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; CP001144; ACH74160.1; -; Genomic_DNA.
DR   RefSeq; WP_000004793.1; NC_011205.1.
DR   AlphaFoldDB; B5FRL4; -.
DR   SMR; B5FRL4; -.
DR   KEGG; sed:SeD_A4741; -.
DR   HOGENOM; CLU_008255_1_1_6; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0052868; F:protein-lysine lysyltransferase activity; IEA:RHEA.
DR   GO; GO:0000049; F:tRNA binding; IEA:TreeGrafter.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   FunFam; 3.30.930.10:FF:000017; Elongation factor P--(R)-beta-lysine ligase; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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   NCBIfam; TIGR00462; genX; 1.
DR   NCBIfam; NF006828; PRK09350.1; 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   PRINTS; PR00982; TRNASYNTHLYS.
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.
FT   CHAIN           1..325
FT                   /note="Elongation factor P--(R)-beta-lysine ligase"
FT                   /id="PRO_1000097905"
FT   BINDING         76..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         100..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         244..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
SQ   SEQUENCE   325 AA;  36870 MW;  F7FBDE09EE388E4C CRC64;
     MSETATWQPS ASIPNLLKRA AIMAEIRRFF ADRGVLEVET PCMSQATVTD IHLFPFETRF
     VGPGHSQGIN LYLMTSPEYH MKRLLAAGCG PVFQLCRSFR NEEMGRHHNP EFTMLEWYRP
     HYDMYRLMNE VDDLLQQVLD CQPAESLSYQ QAFQRHLEID PLSADKTQLR EAAAKLDLSN
     IADTEEDRDT LLQLLFTMGV EPHIGKEKPT FIYHFPASQA SLAQISTEDH RVAERFEVYY
     KGIELANGFH ELTDAREQQQ RFEQDNRKRA ARGLPQQPID QNLLDALAAG LPDCSGVALG
     IDRLVMLALG AESLADVIAF TVDRA
//