Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Vitamin 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.

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Maltose 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.

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

N-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.

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Outer 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 [...]

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Outer 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.

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Outer membrane porin G; Forms channels functionally larger than those of classical porins.

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Outer membrane porin L; Outer membrane channel protein that allows an efficient diffusion of low-molecular-weight solutes such as small sugars and tetraglycine. However, the specific substrate recognized by the OmpL channel is unknown; Belongs to the oligogalacturonate-specific porin KdgM (TC 1.B.35) family. OmpL subfamily.

Vitamin 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.

Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.

Vitamin 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.

TonB-dependent outer membrane ferric citrate transporter and signal transducer; FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system.

Vitamin 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.

Ferrienterobactin 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.

Vitamin 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.

Catecholate 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.

Vitamin 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.

Maltose 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.

Vitamin 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.

N-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.

Vitamin 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.

Outer 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 [...]

Vitamin 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.

Outer 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.

Vitamin 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.

Outer membrane porin G; Forms channels functionally larger than those of classical porins.

Vitamin 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.

Outer membrane porin L; Outer membrane channel protein that allows an efficient diffusion of low-molecular-weight solutes such as small sugars and tetraglycine. However, the specific substrate recognized by the OmpL channel is unknown; Belongs to the oligogalacturonate-specific porin KdgM (TC 1.B.35) family. OmpL subfamily.

Vitamin 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.

Translocation 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.

Vitamin 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.

Transport 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.

Vitamin 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.

Putative iron outer membrane transporter; Probable receptor, TonB-dependent.