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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
fhuEOuter-membrane receptor for ferric coprogen and ferric-rhodotorulic acid; Required for the uptake of Fe(3+) via coprogen, ferrioxamine B, and rhodotorulic acid (729 aa)    
Predicted Functional Partners:
Ferric enterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D
Membrane spanning protein in tonb-exbb-exbd transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]
Membrane spanning protein in tonb-exbb-exbd complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB
Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB
Membrane spanning protein in tonb-exbb-exbd complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates
Tonb-dependent outer membrane ferric citrate transporter and signal transducer; FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system
Enterobactin synthase multienzyme complex component, atp-dependent; Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE)
Enterobactin/ferrienterobactin esterase; Upon internalization, ferric enterobactin is processed via an exquisitely specific pathway that is dependent on FES activity, making iron available for metabolic use
Anti-sigma transmembrane signal transducer for ferric citrate transport; Regulation of iron dicitrate transport. In the absence of citrate FecR inactivates fecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm
iron(3+)-hydroxamate import ABC transporter periplasmic binding protein; Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin
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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