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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
yebCannotation not available (246 aa)    
Predicted Functional Partners:
Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Also mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (PubMed:4292198, PubMed:4579631). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase . In vitro, can also use the non-natural amino acid azatyrosine .
Involved in the regulation of ptsG expression by binding and inactivating Mlc
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. (Microbial infection) Promotes the tRNase activity of CdiA-CT from E.coli strain EC869 (CdiA-CT-EC869); required in vivo but less so in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor capacity of this protein does not seem to be needed as no GTP hydrolysis occurs during tRNA cleavage. Also required in vivo for toxic ac [...]
Malonyl CoA-acyl carrier protein transacylase; Enzyme; Fatty acid and phosphatidic acid biosynthesis; Belongs to the FabD family
This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8 . In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA . The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA . Acts as a peptidyl-tRNA hydrolase . In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). ECO:0000269|PubMe [...]
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. 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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