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folM folM rfbC rfbC rfbD rfbD ompC ompC yfaL yfaL fadL fadL php php waaL waaL wecA wecA wzzE wzzE fhuA fhuA tsx tsx ompF ompF ompA ompA
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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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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:
folMDihydromonapterin reductase, NADPH-dependent; Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate. (240 aa)
rfbCdTDP-4-deoxyrhamnose-3,5-epimerase; Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family. (185 aa)
rfbDdTDP-L-rhamnose synthase, NAD(P)-dependent dTDP-4-dehydrorhamnose reductase subunit; Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS) (Probable). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity). RmlD uses NADH and NADPH nearly equally well (By similarity); Belongs to the dTDP-4-dehydrorhamnose reductase family. (299 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)
yfaLAdhesin; Probably an autotransporter. (1250 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)
phpPhosphotriesterase homology protein; Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate. No enzymatic activity was detected with any of these non-specific substrates. (292 aa)
waaLO-antigen ligase; Adds the O-antigen on the glucose group of LPS. (419 aa)
wecAUDP-GlcNAc:undecaprenylphosphate GlcNAc-1-phosphate transferase; Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the first lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis, and an acceptor for the addition of subsequent sugars to complete the biosynthesis of O-antigen lipopolysaccharide (LPS) in many E.coli O types. The apparent affinity of WecA for the polyisoprenyl phosphate substrates increases with the [...] (367 aa)
wzzEEntobacterial Common Antigen (ECA) polysaccharide chain length modulation protein; Modulates the polysaccharide chain length of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). (348 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)
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)
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)
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)
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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