UniProt Accession

 EPMA_ECOLI; P0A8N7; P03812; P78141; Q2M6E7; Q8XDP9 

Genbank Protein ID

 X59988; U14003; U00096; AP009048; J01611 

Genbank Nucleotide ID

 CAA42604.1; AAA97054.1; AAC77115.2; BAE78159.1; AAA23436.2 

Protein Name

 Elongation factor P--(R)-beta-lysine ligase 

Protein Synonyms/Alias

 EF-P--(R)-beta-lysine ligase; EF-P post-translational modification enzyme A; EF-P-lysine lysyltransferase; GX 

Gene Name

 epmA 

Gene Synonyms/Alias

 genX; poxA; yjeA; b4155; JW4116 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
166	IDPLSADKTQLREVA	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 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'. (R)-beta-lysine is 100-fold more efficient as a substrate than either (S)-beta-lysine or L-alpha- lysine. Cannot ligate lysine to any tRNA. 

Sequence Annotation

 NP_BIND 100 102 ATP.
 NP_BIND 244 245 ATP.
 REGION 76 78 Substrate binding.
 BINDING 109 109 ATP; via amide nitrogen and carbonyl
 BINDING 118 118 Substrate.
 BINDING 251 251 Substrate.
 BINDING 300 300 ATP; via amide nitrogen.  

Keyword

 3D-structure; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 325 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:HAMAP.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004824; F:lysine-tRNA ligase activity; IEA:InterPro.
 GO:0052868; F:protein-lysine lysyltransferase activity; IDA:EcoCyc.
 GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
 GO:0071915; P:protein-lysine lysylation; IDA:EcoCyc.
 GO:0072581; P:protein-N6-(L-lysyl)-L-lysine modification to protein-N6-(beta-lysyl)-L-lysine; IDA:EcoCyc. 

Interpro

 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR004525; EpmA.
 IPR018149; Lys-tRNA-synth_II_C. 

Pfam

 PF00152; tRNA-synt_2 

SMART

  

PROSITE

 PS50862; AA_TRNA_LIGASE_II 

PRINTS

 PR00982; TRNASYNTHLYS.