Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
Engineering the Osmotic State of Pseudomonas putida KT2440 for Efficient Cell Disruption and Downstream Processing of Poly(3-Hydroxyalkanoates)
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OprF is a major outer membrane porin in Pseudomonas putida KT2440
"Then the major outer membrane porin OprF and the specific porin OprE were overproduced during PHA producing conditions on decanoate-grown cells."
Engineered Membrane Vesicle Production via oprF or oprI Deletion Has Distinct Phenotypic Effects in Pseudomonas putida
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Deletion of oprF increases vesiculation and membrane permeability
"In contrast, deletion of oprF, relative to wild type, generated up to a 4-fold increase in MVs but diminished growth, permeabilized membranes, and increased cytosolic protein packaging."
Pseudomonas aeruginosa porin OprF exists in two different conformations
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Canonical OprF is a nonspecific porin that forms large channels
"The major nonspecific porin of Pseudomonas aeruginosa, OprF, produces a large channel yet allows only a slow diffusion of various solutes."
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Only a minority of OprF molecules adopt the open channel state
"only about 5% of the OprF population produced open channels."
Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa
Manual fallback deep research on oprF in Pseudomonas putida KT2440
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OprF is the major outer membrane porin and supports envelope integrity
"OprF is the major outer membrane porin of Pseudomonas putida KT2440 and its loss causes membrane permeabilization and hypervesiculation."
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OprF has canonical OprF/OmpA family architecture
"The Q88L46 UniProt entry assigns a 24-aa signal peptide, an N-terminal outer membrane beta-barrel region, and a C-terminal OmpA-like domain (residues 225-343)."
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The calcium ion binding annotation is weak and likely non-core
"The InterPro-derived calcium ion binding annotation is weak: I found no direct biochemical evidence that KT2440 OprF binds calcium, and the predicted thrombospondin type 3 repeat appears non-core relative to the conserved porin/OmpA architecture."