All terms in GO

Label Id Description
obsolete hemaglutinin autotransporter activity GO_0015476 [OBSOLETE. Enables the transfer of hemaglutinin from the periplasm to the external milieu; the hemaglutinin and the porin are the N- and C-terminal regions of the same protein, respectively.]
obsolete receptor porin activity GO_0015477 [OBSOLETE. A porin of the bacterial outer membrane that forms transmembrane pores and transports relatively large molecules from the external milieu to the periplasm in an energized process. Energizing of transport across the outer membrane requires a heterotrimeric complex of proteins, the TonB-ExbB-ExbD complex, or in some cases, the TolA-TolQ-TolR complex. Energizing requires proton motive force across the cytoplasmic membrane.]
autotransporter activity GO_0015474 [Transports a passenger protein from the periplasm to the external milieu; the passenger protein and the porin are the N- and C-terminal regions of the same protein, respectively.]
obsolete adhesin autotransporter activity GO_0015475 [OBSOLETE. Enables the transfer of adhesin from the periplasm to the external milieu; the adhesin and the porin are the N- and C-terminal regions of the same protein, respectively.]
obsolete fimbrium-specific chaperone activity GO_0015472 [OBSOLETE. Assists in the correct assembly of fimbria, extracellular organelles that are used to attach a bacterial cell to a surface, but is not a component of the fimbrium when performing its normal biological function.]
fimbrial usher porin activity GO_0015473 [A porin that acts in the assembly of fimbria together with fimbrial chaperone.]
obsolete bacteriocin activity GO_0015470 [OBSOLETE. Polypeptide antibiotic secreted by bacteria and able to kill bacteria of susceptible strains after absorption by specific cell surface receptor.]
nucleoside-specific channel forming porin activity GO_0015471 [Enables the energy independent passage of nucleoside, sized less than 1000 Da, across a membrane. The transmembrane portions of porins consist exclusively of beta-strands which form a beta-barrel. They are found in the outer membranes of Gram-negative bacteria, mitochondria, plastids and possibly acid-fast Gram-positive bacteria.]
melibiose transmembrane transporter activity GO_0015156 [Enables the transfer of melibiose from one side of a membrane to the other. Melibiose is the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose and occurs as a constituent of the trisaccharide raffinose or in the exudates and nectaries of a number of plants.]
glucuronide:cation symporter activity GO_0015488 [Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: glucuronide(out) + monovalent cation(out) = glucuronide(in) + monovalent cation(in).]
glycoside-pentoside-hexuronide:cation symporter activity GO_0015486 [Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: (glycoside, pentoside or hexuronide)(out) + monovalent cation(out) = (glycoside, pentoside or hexuronide)(in) + monovalent cation(in). The cation is Na+, Li+ or H+.]
glucuronoside transmembrane transporter activity GO_0015164 [Enables the transfer of a glucuronosides from one side of a membrane to the other. Glucuronosides are any compound formed by combination of glycosidic linkage of a hydroxy compound (e.g. an alcohol or a saccharide) with the anomeric carbon atom of glucuronate.]
cholesterol binding GO_0015485 [Binding to cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.]
long-chain fatty acid transporting porin activity GO_0015483 [Enables the transfer of a long-chain fatty acid from one side of a membrane to the other. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons. This transporter is a porin and so enables the energy independent passage of substances, sized less than 1000 Da, across a membrane. The transmembrane portions of porins consist exclusively of beta-strands which form a beta-barrel. They are found in the outer membranes of Gram-negative bacteria, mitochondria, plastids and possibly acid-fast Gram-positive bacteria.]
obsolete hemolysin activity GO_0015484 [OBSOLETE. Any substance that causes the lysis of red blood cells.]
maltose transporting porin activity GO_0015481 [Enables the transfer of maltose from one side of a membrane to the other. Maltose is the disaccharide 4-O-alpha-D-glucopyranosyl-D-glucopyranose, an intermediate in the enzymatic breakdown of glycogen and starch. This transporter is a porin so enables the energy independent passage of substances, sized less than 1000 Da, across a membrane. The transmembrane portions of porins consist exclusively of beta-strands which form a beta-barrel. They are found in the outer membranes of Gram-negative bacteria, mitochondria, plastids and possibly acid-fast Gram-positive bacteria.]
obsolete voltage-gated anion channel porin activity GO_0015482 [OBSOLETE. This term was not defined before being made obsolete.]
obsolete secretin (sensu Bacteria) GO_0015480 [OBSOLETE. Secretins are Gram-negative bacterial outer membrane proteins that form multimeric pores through which macromolecules, usually proteins, can pass. Form homomultimeric ring structures, 10-20 subunits per complex, with large central pores (inner diameters of 5-10 nm).]
pantothenate:sodium symporter activity GO_0015498 [Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: pantothenate(out) + Na+(out) = pantothenate(in) + Na+(in).]
putrescine:ornithine antiporter activity GO_0015496 [Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: putrescine(out) + ornithine(in) = putrescine(in) + ornithine(out).]