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lamB lamB btuB btuB mrr mrr wecB wecB waaG waaG waaC waaC tolC tolC rpoS rpoS fadL fadL ompC ompC rrrQ rrrQ yncD yncD mcrA mcrA ptsG ptsG ompA ompA ompF ompF fepA fepA nfrA nfrA rrrD rrrD tsx tsx fhuA fhuA lptD lptD
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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
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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)
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)
mrrMethylated adenine and cytosine restriction protein; Involved in the acceptance of foreign DNA which is modified. Restricts both adenine- and cytosine-methylated DNA. (304 aa)
wecBUDP-N-acetyl glucosamine-2-epimerase; Catalyzes the reversible epimerization at C-2 of UDP-N- acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP- N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption. (376 aa)
waaGUDP-glucose:(heptosyl)lipopolysaccharide alpha-1,3-glucosyltransferase; Involved in the addition of the first glucose residue to the lipopolysaccharide core; Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily. (374 aa)
waaCADP-heptose:LPS heptosyl transferase I; Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA; Belongs to the glycosyltransferase 9 family. (319 aa)
tolCTransport channel; Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. (493 aa)
rpoSRNA polymerase, sigma S (sigma 38) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. Controls, positively or negatively, the expression of several hundred genes, which are mainly involved in metabolism, transport, regulation and stress management. (330 aa)
fadLLong-chain fatty acid outer membrane transporter; Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel; Belongs to the OmpP1/FadL family. (446 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)
rrrQQin prophage; Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity; Belongs to the glycosyl hydrolase 24 family. (177 aa)
yncDPutative iron outer membrane transporter; Probable receptor, TonB-dependent. (700 aa)
mcrAPutative 5-methylcytosine/5-hydroxymethylcytosine-specific restriction nuclease; Restriction of 5-methyl and 5-hydroxymethylcytosines at the specific DNA sequence C(me)CGG. (277 aa)
ptsGFused glucose-specific PTS enzymes: IIB component/IIC component; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport. Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc. (477 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)
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)
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)
nfrABacteriophage N4 receptor, outer membrane subunit; (Microbial infection) Allows N4 phage attachment by binding to the viral non-contractile sheath protein. (990 aa)
rrrDDLP12 prophage; Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Exhibits lytic activity against E.coli and S.typhi cell wall substrate; Belongs to the glycosyl hydrolase 24 family. (165 aa)
tsxNucleoside channel, receptor of phage T6 and colicin K; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases. In addition, constitutes the receptor for colicin K and phage T6. Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. (294 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)
lptDLPS assembly OM complex LptDE, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance. (784 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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