STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
epmAElongation factor P--(R)-beta-lysine ligase; 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 (325 aa)    
Predicted Functional Partners:
Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed pol [...]
L-lysine 2,3-aminomutase; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)- alpha-lysine as a substrate; Belongs to the radical SAM superfamily. KamA family
Elongation factor P hydroxylase; Is involved in the final hydroxylation step of the post- translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine
DNA utilization protein YhgH; Required for the use of extracellular DNA as a nutrient. Has been suggested to be involved in gluconate metabolism
annotation not available
Energy-dependent translational throttle protein EttA; A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E site where it modulates the state of the translating ribosome during subunit translocation. Stimulates dipeptide bond synthesis in the presence of ATP (cell in high energy state), but inhibits dipeptide synthesis in the presence of ADP (cell in low energy state), and thus may control tran [...]
Release factor glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation facto [...]
Inner membrane transporter YjeM; Putative transport
Putative elongation factor; Protein involved in translation
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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