Q0T9N4 EPMA_ECOL5 Elongation factor P--(R)-beta-lysine ligase EF-P--(R)-beta-lysine ligase 6.3.2.- EF-P post-translational modification enzyme A EF-P-lysine lysyltransferase epmA yjeA ECP_4401 Escherichia coli O6:K15:H31 (strain 536 / UPEC) Bacteria Pseudomonadati Pseudomonadota Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] 536 / UPEC With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'. D-beta-lysine + L-lysyl-[protein] + ATP = N(6)-((3R)-3,6-diaminohexanoyl)-L-lysyl-[protein] + AMP + diphosphate + H(+) Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. ATP-binding Ligase Nucleotide-binding substrate ATP ATP substrate ATP substrate ATP MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License