LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The ompA-like transmembrane domain is present in a number of different outer membrane proteins of several Gram-negative bacteria. Many of the proteins having this domain in the N-terminal also have the conserved bacterial outer membrane protein domain at the C terminus. 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. 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 [].OmpA consists of a regular, extended eight-stranded β-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. The cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of β-barrels [ ]. The β-barrel membrane anchor appears to be the outer membrane equivalent of the single-chain α-helix anchor of the inner membrane. |
| Short Name | OmpA-like_TM_dom |
