P0A8N7 · EPMA_ECOLI

Function

function

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

Caution

Was originally suggested to be a tRNA synthase, however its lack of an anticodon-binding domain made this highly unlikely.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
213 μM(R)-beta-lysine
8600 μML-alpha-lysine
6950 μM(S)-beta-lysine
206 μMATP
kcat is 36 min-1 for the amino acid activation reaction with (R)-beta-lysine as substrate.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site76-78substrate
Binding site100-102ATP (UniProtKB | ChEBI)
Binding site109ATP (UniProtKB | ChEBI)
Binding site118substrate
Binding site244-245ATP (UniProtKB | ChEBI)
Binding site251substrate
Binding site300ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionacid-ammonia (or amide) ligase activity
Molecular FunctionATP binding
Molecular Functionlysine-tRNA ligase activity
Molecular Functionprotein homodimerization activity
Molecular Functionprotein-lysine lysyltransferase activity
Molecular FunctiontRNA binding
Biological Processcellular response to acidic pH
Biological Processlysyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Elongation factor P--(R)-beta-lysine ligase
  • EC number
  • Short names
    EF-P--(R)-beta-lysine ligase
  • Alternative names
    • EF-P post-translational modification enzyme A
    • EF-P-lysine lysyltransferase
    • GX

Gene names

    • Name
      epmA
    • Synonyms
      genX, poxA, yjeA
    • Ordered locus names
      b4155, JW4116

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0A8N7
  • Secondary accessions
    • P03812
    • P78141
    • Q2M6E7
    • Q8XDP9

Proteomes

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Cells have a reduced pyruvate oxidase activity and a reduced growth rate. Cells lack CadA activity (lysine decarboxylase).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis50No effect on lysylation activity.
Mutagenesis76Loss of catalytic activity.
Mutagenesis100Loss of lysylation activity.
Mutagenesis102No effect on lysylation activity.
Mutagenesis103Loss of lysylation activity.
Mutagenesis108Severe reduction in lysylation activity.
Mutagenesis185Slight reduction in lysylation activity.
Mutagenesis193Slight reduction in lysylation activity.
Mutagenesis244Loss of lysylation activity.
Mutagenesis247Loss of lysylation activity.
Mutagenesis29896% increase in the affinity for L-alpha-lysine. 4-fold decrease in the catalytic efficiency of the (R)-beta-lysine activation reaction.
Mutagenesis303Loss of lysylation activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001527191-325Elongation factor P--(R)-beta-lysine ligase

Proteomic databases

Interaction

Subunit

Homodimer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P0A8N7aceE P0AFG82EBI-562598, EBI-542683

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    325
  • Mass (Da)
    36,976
  • Last updated
    2005-06-07 v1
  • Checksum
    F72B535CCA23E4CC
MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA

Sequence caution

The sequence AAA97054.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict78in Ref. 5; AAA23436
Sequence conflict144in Ref. 5; AAA23436

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X59988
EMBL· GenBank· DDBJ
CAA42604.1
EMBL· GenBank· DDBJ
Genomic DNA
U14003
EMBL· GenBank· DDBJ
AAA97054.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
U00096
EMBL· GenBank· DDBJ
AAC77115.2
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE78159.1
EMBL· GenBank· DDBJ
Genomic DNA
J01611
EMBL· GenBank· DDBJ
AAA23436.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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