Part:BBa_K864204

OmpF

Information contributed by City of London UK (2021)

Part information is collated here to help future users of the BioBrick registry.

Metadata:

Group: City of London UK 2021
Author: Lucas Ng
Summary: Added information collated from existing scientific studies

This matrix porin forms cell pores facilitating passive diffusion of small molecules across the outer cell membrane. ^[1]

It forms a mixed heterotrimer with osmoporin OmpC which acts as the outer membrane receptor for the CdiA-EC536 toxin, via polymorphisms in OmpC's extracellular loops 4 and 5 ^[2]. It also acts as a receptor for the bacteriophage T2 and is the major receptor for colicin E5.

References

↑ Duval, Valérie, Hervé Nicoloff, and Stuart B. Levy. 2009. “Combined Inactivation of Lon and YcgE Decreases Multidrug Susceptibility by Reducing the Amount of OmpF Porin in Escherichia Coli.” Antimicrobial Agents and Chemotherapy 53 (11): 4944–48. https://doi.org/10.1128/AAC.00787-09.
↑ Beck, Christina M., Julia L. E. Willett, David A. Cunningham, Jeff J. Kim, David A. Low, and Christopher S. Hayes. 2016. “CdiA Effectors from Uropathogenic Escherichia Coli Use Heterotrimeric Osmoporins as Receptors to Recognize Target Bacteria.” PLoS Pathogens 12 (10): e1005925. https://doi.org/10.1371/journal.ppat.1005925.

[1] Duval, Valérie, Hervé Nicoloff, and Stuart B. Levy. 2009. “Combined Inactivation of Lon and YcgE Decreases Multidrug Susceptibility by Reducing the Amount of OmpF Porin in Escherichia Coli.” Antimicrobial Agents and Chemotherapy 53 (11): 4944–48. https://doi.org/10.1128/AAC.00787-09.

[2] Beck, Christina M., Julia L. E. Willett, David A. Cunningham, Jeff J. Kim, David A. Low, and Christopher S. Hayes. 2016. “CdiA Effectors from Uropathogenic Escherichia Coli Use Heterotrimeric Osmoporins as Receptors to Recognize Target Bacteria.” PLoS Pathogens 12 (10): e1005925. https://doi.org/10.1371/journal.ppat.1005925.

[1]

[2]