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lamB lamB yncD yncD bluF bluF fhuE fhuE fiu fiu fepA fepA fhuA fhuA ftsY ftsY btuB btuB fecA fecA cirA cirA
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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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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
lamBMaltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. (446 aa)
yncDPutative iron outer membrane transporter; Probable receptor, TonB-dependent. (700 aa)
bluFAnti-repressor for YcgE, blue light-responsive; Binds to and releases the BluR repressor from its bound DNA target in a blue light-dependent (470 nm) fashion. A shift to low temperature also triggers a BluF-mediated relief of repression by BluR, suggesting BluF may serve as a thermometer. Blue light may act to increase the affinity of BluF for BluR, allowing it to be released from its operator. The protein has a reversible photocycle, and undergoes structural changes, probably in the EAL domain, in response to light. (403 aa)
fhuEFerric-rhodotorulic acid outer membrane transporter; Required for the uptake of Fe(3+) via coprogen, ferrioxamine B, and rhodotorulic acid. (729 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)
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)
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)
ftsYSignal Recognition Particle (SRP) receptor; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components. (497 aa)
btuBVitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. (614 aa)
fecATonB-dependent outer membrane ferric citrate transporter and signal transducer; FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system. (774 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)
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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