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lpp lpp nanC nanC fecA fecA tamA tamA lamB lamB btuB btuB pldA pldA tolC tolC ompC ompC yddB yddB yncD yncD ompG ompG csgG csgG pgaA pgaA ompA ompA fiu fiu fepA fepA
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second shell of interactors
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proteins of unknown 3D structure
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lppMurein lipoprotein; An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most adundant cellular protein, there can be up to 10(6) Lpp molecules pe [...] (78 aa)
nanCN-acetylnuraminic acid outer membrane channel protein; Outer membrane channel protein allowing the entry of N- acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria (Probable). NanC proteins form high- conductance channels which are open at low membrane potentials and which have a weak anion selectivity; Belongs to the oligogalacturonate-specific porin KdgM (TC 1.B.35) family. NanC subfamily. (238 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)
tamATranslocation and assembly module for autotransporter export, outer membrane subunit; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Allows substrate (Ag43, AC P39180) to initiate penetration into the outer membrane; TamB is not necessary but may regulate this activity. Has anion selective channel- forming ability, but the physiological relevance of this activity is unclear ; Belongs to the TamA family. (577 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)
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)
pldAOuter membrane phospholipase A; Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins. (289 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)
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)
yddBPutative TonB-dependent outer membrane receptor; To H.influenzae HI_1369. (790 aa)
yncDPutative iron outer membrane transporter; Probable receptor, TonB-dependent. (700 aa)
ompGOuter membrane porin G; Forms channels functionally larger than those of classical porins. (301 aa)
csgGCurli production assembly/transport outer membrane lipoprotein; May be involved in the biogenesis of curli organelles. (277 aa)
pgaABiofilm adhesin polysaccharide PGA secretin; Exports the biofilm adhesin polysaccharide poly-beta-1,6-N- acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin. (807 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)
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)
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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