Anti-ompF antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The ompF protein known as Outer membrane protein F serves as a porin in the outer membrane of Escherichia coli. It facilitates the passive diffusion of small molecules across the cell membrane. This protein has a trimeric structure where each monomer forms a beta-barrel. Each of the monomers has a mass of about 38 kDa. The ompF protein is typically expressed in response to varying environmental factors like osmolarity and is important for regulating molecule entry into the bacterial cell.

Biological function summary

OmpF plays a significant role in maintaining homeostasis and nutrient uptake in bacteria. It forms part of the beta-barrel assembly machinery complex which handles the insertion and folding of beta-barrel proteins into the outer membrane. This protein adjusts bacteria's permeability properties ensuring necessary ions and small nutrients reach the cell’s interior while controlling the access of harmful substances.

Pathways

OmpF participates in nutrient uptake and ion transport pathways significantly affecting bacterial survival and adaptation processes. OmpF interacts with other proteins in the porin family such as ompC which collectively regulate ion passage and osmotic balance within the bacterial cell envelope. These actions occur in pathways related to membrane permeability which are vital for bacteria responding to environmental stress.

Associated diseases and disorders

OmpF has a linkage to antibiotic resistance mechanisms in pathogenic bacteria. Alterations in the ompF protein or expression can reduce antibiotic susceptibility complicating treatment of infections caused by Escherichia coli. This protein has connections with various resistance proteins where modulating such pathways may enhance antibiotic effectiveness. Understanding its role and interactions can guide strategies to counteract antimicrobial resistance in clinical settings.