STRINGSTRING
emrA emrA emrK emrK acrD acrD emrB emrB tolC tolC acrF acrF mdtF mdtF acrA acrA acrB acrB macA macA macB macB msbA msbA
Nodes:
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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emrAMultidrug efflux system; Part of the tripartite efflux system EmrAB-TolC, which confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol and nalidixic acid. EmrA is a drug-binding protein that provides a physical link between EmrB and TolC; Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. (390 aa)
emrKMultidrug resistance efflux pump membrane fusion protein; Part of the tripartite efflux system EmrYK-TolC, which confers resistance to various drugs. (387 aa)
acrDAminoglycoside/multidrug efflux system; Participates in the efflux of aminoglycosides. Confers resistance to a variety of these substances. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. (1037 aa)
emrBMultidrug efflux system protein; Part of the tripartite efflux system EmrAB-TolC, which confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol and nalidixic acid. (512 aa)
tolCTransport channel; 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. (493 aa)
acrFMultidrug efflux system protein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. (1034 aa)
mdtFAnaerobic multidrug efflux transporter, ArcA-regulated; 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; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. (1037 aa)
acrAMultidrug efflux system; 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. (397 aa)
acrBMultidrug efflux system protein; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. (1049 aa)
macAMacrolide transporter membrane fusion protein (MFP) component; Part of the tripartite efflux system MacAB-TolC. MacA stimulates the ATPase activity of MacB by promoting the closed ATP- bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC. 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, MacA binds tightly rough-core lipopolysaccharide (R-LPS), suggesting that the system co [...] (371 aa)
macBMacrolide ABC transporter peremase/ATPase; 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. Belongs to the ABC transporter superfamily. Macrolide exporte [...] (648 aa)
msbALipid ABC transporter permease/ATPase; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. Belongs to the ABC transporter superfamily. Lipid exporter (TC 3.A.1.106) family. (582 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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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