v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The OmpA outer membrane proteins in this group all contain the OmpA-like transmembrane domain at the N-terminal and the conserved bacterial outer membrane protein domain at the C-terminal. The outer membrane protein A of Escherichia coli (OmpA), is one of the most studied proteins in this group [ ]. It has a multifunctional role. OmpA is required for the action of colicins K and L and for the stabilisation of mating aggregates in conjugation. OmpA may be involved in the maintenance of the position of the peptidoglycan cell wall in the periplasm by non-covalent interaction with TolR []. These proteins are implicated as a secondary receptor for a number of T-even like phages, for example, during phage Sf6 infection, it requires both lipopolysaccharide and OmpA []. In addition, OmpA can act as a porin with low permeability that allows slow penetration of small solutes []. |
| Short Name | OmpA |