Poly-beta-1,6 N-acetyl-D-glucosamine export porin PgaA (IPR023870)

Short name: PGA_export_porin_PgaA

Overlapping homologous superfamilies


Family relationships



Members of this protein family are the poly-beta-1,6 N-acetyl-D-glucosamine (PGA) export porin PgaA of Gram-negative bacteria. There is no counterpart in the poly-beta-1,6 N-acetyl-D-glucosamine biosynthesis systems of Gram-positive bacteria such as Staphylococcus epidermidis. The PGA polysaccharide adhesin is a critical determinant of biofilm formation. This enzyme exports PGA across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin [PMID: 15090514,PMID: 19460094].

This outer membrane protein contains a predicted C-terminal beta-barrel porin domain and a N-terminal periplasmic superhelical domain containing tetratricopeptide repeats, which may mediate protein-protein interactions, perhaps with PgaB [PMID: 18359807].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:1901515 poly-beta-1,6-N-acetyl-D-glucosamine transmembrane transporter activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.