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
acrDParticipates in the efflux of aminoglycosides. Confers resistance to a variety of these substances. (1037 aa)    
Predicted Functional Partners:
AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm
Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:18955484,
Part of the tripartite efflux system MdtEF-TolC, which confers resistance to compounds such as rhodamine 6G, erythromycin, doxorubicin, ethidium bromide, TPP, SDS, deoxycholate, crystal violet and benzalkonium
The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.
Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis
Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. ECO:0000269|PubMed:17214741, ECO:0000269|PubMed:18955484,
Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents.
Part of the tripartite efflux system EmrYK-TolC, which confers resistance to various drugs
Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress . Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression . Activates the mdtABCD and probably the CRISPR-Cas casABCDE-ygbT-ygbF operon .
Multidrug resistance pump that participates in a low energy shock adaptive response
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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