ompF outer membrane porin F [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: ompF
Official Full Name: outer membrane porin F
Primary source: ECOCYC:EG10671
Locus tag: b0929
See related: ASAP:ABE-0003153
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: cmlB; cry; ECK0920; nfxB; tolF
Summary: Trimeric. [More information is available at EcoGene: EG10671]. OmpF is a member of the General Bacterial Porin (GBP) family. [More information is available at EcoCyc: EG10671].
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Genomic context

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Sequence:: NC_000913.3 (985894..986982, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Study of the early response of Escherichia coli lpcA and ompF mutants to ciprofloxacin.
Title: Study of the early response of Escherichia coli lpcA and ompF mutants to ciprofloxacin.
Designer Outer Membrane Protein Facilitates Uptake of Decoy Molecules into a Cytochrome P450BM3-Based Whole-Cell Biocatalyst.
Title: Designer Outer Membrane Protein Facilitates Uptake of Decoy Molecules into a Cytochrome P450BM3-Based Whole-Cell Biocatalyst.
A protocol for production of perdeuterated OmpF porin for neutron crystallography.
Title: A protocol for production of perdeuterated OmpF porin for neutron crystallography.
Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.
Title: Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.
OmpF Downregulation Mediated by Sigma E or OmpR Activation Confers Cefalexin Resistance in Escherichia coli in the Absence of Acquired beta-Lactamases.
Title: OmpF Downregulation Mediated by Sigma E or OmpR Activation Confers Cefalexin Resistance in Escherichia coli in the Absence of Acquired β-Lactamases.
Trimeric porins, such as ompF, have specific lipopolysaccharide binding sites that are essential for porin biogenesis.
Title: Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.
Klebsiella pneumoniae OmpK35 and OmpK36 produced larger more permeable channels than their Escherichia coli homologs OmpF and OmpC.
Title: Klebsiella pneumoniae Major Porins OmpK35 and OmpK36 Allow More Efficient Diffusion of β-Lactams than Their Escherichia coli Homologs OmpF and OmpC.
The results suggest that trimerization is crucial for both structure and function of general porin OmpF in E. coli, whereas being trimer in substrate-specific channel OprP supports a pore function in Pseudomonas aeruginosa.
Title: Why do the outer membrane proteins OmpF from E. coli and OprP from P. aeruginosa prefer trimers? Simulation studies.
Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block
Title: Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block.
The site of lipopolysaccharide binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF.
Title: The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.

Submit: New GeneRIF Correction See all GeneRIFs (26)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables colicin transmembrane transporter activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables disordered domain specific binding	IPI Inferred from Physical Interaction more info	PubMed
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables lipid binding	IDA Inferred from Direct Assay more info	PubMed
enables lipopolysaccharide binding	IDA Inferred from Direct Assay more info	PubMed
enables monoatomic ion channel activity	IDA Inferred from Direct Assay more info	PubMed
enables porin activity	IBA Inferred from Biological aspect of Ancestor more info
enables porin activity	IEA Inferred from Electronic Annotation more info
enables porin activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables porin activity	TAS Traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in bacteriocin transport	IEA Inferred from Electronic Annotation more info
involved_in monoatomic ion transmembrane transport	IDA Inferred from Direct Assay more info	PubMed
involved_in monoatomic ion transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in monoatomic ion transmembrane transport	TAS Traceable Author Statement more info	PubMed
involved_in monoatomic ion transport	IEA Inferred from Electronic Annotation more info
involved_in protein homotrimerization	IDA Inferred from Direct Assay more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cell outer membrane	IDA Inferred from Direct Assay more info	PubMed
located_in cell outer membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
part_of monoatomic ion channel complex	IDA Inferred from Direct Assay more info	PubMed
part_of pore complex	IBA Inferred from Biological aspect of Ancestor more info
part_of pore complex	IDA Inferred from Direct Assay more info	PubMed
part_of pore complex	IEA Inferred from Electronic Annotation more info