P0A8N7 · EPMA_ECOLI
- ProteinElongation factor P--(R)-beta-lysine ligase
- GeneepmA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids325 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
213 μM | (R)-beta-lysine | |||||
8600 μM | L-alpha-lysine | |||||
6950 μM | (S)-beta-lysine | |||||
206 μM | ATP |
kcat is 36 min-1 for the amino acid activation reaction with (R)-beta-lysine as substrate.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 76-78 | substrate | ||||
Sequence: SPE | ||||||
Binding site | 100-102 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RNE | ||||||
Binding site | 109 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 118 | substrate | ||||
Sequence: Y | ||||||
Binding site | 244-245 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EL | ||||||
Binding site | 251 | substrate | ||||
Sequence: E | ||||||
Binding site | 300 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | acid-ammonia (or amide) ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | lysine-tRNA ligase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein-lysine lysyltransferase activity | |
Molecular Function | tRNA binding | |
Biological Process | cellular response to acidic pH | |
Biological Process | lysyl-tRNA aminoacylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation factor P--(R)-beta-lysine ligase
- EC number
- Short namesEF-P--(R)-beta-lysine ligase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A8N7
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 50 | No effect on lysylation activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 76 | Loss of catalytic activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 100 | Loss of lysylation activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 102 | No effect on lysylation activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 103 | Loss of lysylation activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 108 | Severe reduction in lysylation activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 185 | Slight reduction in lysylation activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 193 | Slight reduction in lysylation activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 244 | Loss of lysylation activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 247 | Loss of lysylation activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 298 | 96% increase in the affinity for L-alpha-lysine. 4-fold decrease in the catalytic efficiency of the (R)-beta-lysine activation reaction. | ||||
Sequence: A → G | ||||||
Mutagenesis | 303 | Loss of lysylation activity. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000152719 | 1-325 | Elongation factor P--(R)-beta-lysine ligase | |||
Sequence: MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA |
Proteomic databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0A8N7 | aceE P0AFG8 | 2 | EBI-562598, EBI-542683 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length325
- Mass (Da)36,976
- Last updated2005-06-07 v1
- ChecksumF72B535CCA23E4CC
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 78 | in Ref. 5; AAA23436 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 144 | in Ref. 5; AAA23436 | ||||
Sequence: A → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |