STRINGSTRING
tolQ tolQ tolR tolR tolB tolB ompF ompF ompW ompW cirA cirA ompC ompC exbD exbD exbB exbB btuB btuB lamB lamB
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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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experimentally determined
Predicted Interactions
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textmining
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Your Input:
tolQMembrane spanning protein in TolA-TolQ-TolR complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. Is also involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. Belongs to the ExbB/TolQ family. (230 aa)
tolRMembrane spanning protein in TolA-TolQ-TolR complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction .The Tol-Pal system is also required for polar localization of chemoreceptors clusters (Probable). There are about 900 TolR molecules per cell. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan [...] (142 aa)
tolBPeriplasmic protein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. Is also involved in the uptake of some colicins A. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. (430 aa)
ompFOuter membrane porin 1a (Ia;b;F); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (362 aa)
ompWOuter membrane protein W; Acts as a receptor for colicin S4. (212 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)
ompCOuter membrane porin protein C; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (367 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)
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)
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)
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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