Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa.
Protein D2 channel of the Pseudomonas aeruginosa outer membrane has a binding site for basic amino acids and peptides.
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Basic amino acids competitively inhibit imipenem diffusion through D2, and D2+ cells take up Thr-Ser-Lys faster than D2- mutants.
"Wild type cells transported tripeptide Thr-Ser-Lys into the"
Outer membrane proteins responsible for the penetration of beta-lactams and quinolones in Pseudomonas aeruginosa.
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Chemically mutagenised latamoxef/quinolone-resistant PAO1 transductants had reduced amounts of four outer membrane proteins (C, D2, E1, E2) together, which lowered OM permeability.
"decreased amounts of outer membrane proteins C, D2, E1, and E2 lowered the"
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The authors conclude only that at least one of the four proteins acts as a porin for the drugs.
"The results suggested that at least one of the four proteins was"
Two-dimensional polyacrylamide gel electrophoresis isolation and microsequencing of Pseudomonas aeruginosa proteins.
Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity.
Substrate specificity within a family of outer membrane carboxylate channels.
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Occ (OprD family) channels are the main route for small water-soluble molecules across the P. aeruginosa outer membrane.
"most of the water-soluble small molecules are thought to be taken up by members of the Outer membrane carboxylic acid channel (Occ) family"