v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | This entry represents a transmembrane beta (8,10)-barrel found in outer membrane proteins such as OmpA, OmpX and NspA, and in the outer membrane enzyme PagP [ ]. OmpA is multifunctional, being required for the action of colicins K and L, and for the stabilisation of mating aggregates in conjugation; it also serves as a receptor for a number of T-even like phages, and can act as a porin with low permeability that allows slow penetration of small solutes [ ]. OmpX is a cation-selective channel that is regulated by osmolarity and by MarA expression []. NspA (Neisseria surface protein A) is an iron-activated membrane protein of unknown function []. The outer membrane enzyme PagP helps pathogenic bacteria to evade the host immune response catalysing palmitate transfer from a phospholipid to a glucosamine unit of lipid A [, ]. |
Short Name | OMP/PagP_b-brl |