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
secMRegulator of seca translation; Regulates secA expression by translational coupling of the secM secA operon. Ribosomes translating the C-terminal region of secM can disrupt an RNA repressor helix that normally blocks secA translation initiation, derepressing the expression of secA. Translational pausing of secM at Pro-166 under secretion-limiting conditions increases the duration of the disruption and thus increases secA expression. This is controlled by interaction of the secM signal peptide with secA and the translocon, possibly by secA pulling the paused secM out of the ribosome. The [...] (170 aa)    
Predicted Functional Partners:
Preprotein translocase subunit, atpase; Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane
Tryptophanase leader peptide; Required for tryptophan-regulated expression of the tna operon. In the presence of free L-Trp release of this nascent peptide by release factor 2 is inhibited and the ribosome stalls with the last amino acid in the P site and a UGA stop codon in the A site. This prevent transcripiton termination factor Rho binding, and thus allows transcription and translation of TnaA and TnaB
Ribonuclease iii; Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, sh [...]
Peptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates . Binds to nascent polypeptide chains via ribosomal protein L23 . Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity
DUF1375 domain-containing putative lipoprotein YidQ; To E.coli YceK
YidC/Oxa1 family membrane protein insertase; Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec- independent subunit c of the F(0)ATP synthase, M13 phage procoat and the N- [...]
annotation not available
Rescues ribosomes stalled at the 3' end of non-stop mRNAs . This activity is crucial when the stalled ribosome cannot be rescued by the SsrA(tmRNA)-SmpB quality control system . Binds the 30S subunit, contacting 16S rRNA with the N-terminus near the decoding center and its C-terminus in the mRNA entry channel; contacts change in the presence of release factor 2 (RF2, also named PrfB) Requires RF2/PrfB to hydrolyze stalled peptidyl-tRNA on the ribosome; recruits and probably helps position RF2/PrfB correctly in the ribosomal A site so RF2's GGQ motif can hydrolyze the peptidyl-tRNA bond [...]
Thiamine kinase; Catalyzes the phosphorylation of thiamine to thiamine phosphate
Periplasmic bacteriophage sensitivity protein dcrb; Required for phage C1 adsorption
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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