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cirA cirA fhuA fhuA fepA fepA fepC fepC fepD fepD fepB fepB fiu fiu tonB tonB exbD exbD exbB exbB argD argD
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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
Your Input:
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)
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)
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)
fepCFerrienterobactin ABC transporter ATPase; Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for energy coupling to the transport system. (271 aa)
fepDFerrienterobactin ABC transporter permease; Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for the translocation of the substrate across the membrane. (334 aa)
fepBFerrienterobactin ABC transporter periplasmic binding protein; Binds ferrienterobactin; part of the binding-protein- dependent transport system for uptake of ferrienterobactin. (318 aa)
fiuCatecholate siderophore receptor; Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492. (760 aa)
tonBMembrane 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 [...] (239 aa)
exbDMembrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. (141 aa)
exbBMembrane 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. (244 aa)
argDBifunctional acetylornithine aminotransferase and succinyldiaminopimelate aminotransferase; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (406 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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