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fhuD fhuD fepA fepA fepB fepB cydB cydB ompA ompA fhuE fhuE cirA cirA soxS soxS uxuR uxuR fhuF fhuF fhuA fhuA dnaK dnaK
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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fhuDIron(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. (296 aa)
fepAFerrienterobactin 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. (746 aa)
fepBFerrienterobactin ABC transporter periplasmic binding protein; Binds ferrienterobactin; part of the binding-protein- dependent transport system for uptake of ferrienterobactin. (318 aa)
cydBCytochrome d terminal oxidase, subunit II; A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (379 aa)
ompAOuter membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...] (346 aa)
fhuEFerric-rhodotorulic acid outer membrane transporter; Required for the uptake of Fe(3+) via coprogen, ferrioxamine B, and rhodotorulic acid. (729 aa)
cirAColicin IA outer membrane receptor and translocator; Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. (663 aa)
soxSSuperoxide response regulon transcriptional activator; Transcriptional activator of the superoxide response regulon of E.coli that includes at least 10 genes such as sodA, nfo, zwf and micF. Binds the DNA sequence 5'-GCACN(7)CAA-3'. It also facilitates the subsequent binding of RNA polymerase to the micF and the nfo promoters. (107 aa)
uxuRFructuronate-inducible hexuronate regulon transcriptional repressor; Repressor for the uxuRBA operon. (257 aa)
fhuFFerric iron reductase involved in ferric hydroximate transport; Involved in the reduction of ferric iron in cytoplasmic ferrioxamine B. (262 aa)
fhuAFerrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system. (747 aa)
dnaKChaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock. (638 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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