Channel forming colicin, C-terminal cytotoxic (IPR000293)

Short name: Channel_colicin_C

Overlapping homologous superfamilies

Domain relationships



Colicins are plasmid-encoded polypeptide toxins produced by and active against Escherichia coli and closely related bacteria. Colicins are released into the environment to reduce competition from other bacterial strains. Colicins bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmic membrane, where they exert their cytotoxic effect, including depolarisation of the cytoplasmic membrane, DNase activity, RNase activity, or inhibition of murein synthesis.

Channel-forming colicins (colicins A, B, E1, Ia, Ib, and N) are transmembrane proteins that depolarize the cytoplasmic membrane, leading to dissipation of cellular energy [PMID: 14731273]. These colicins contain at least three domains: an N-terminal translocation domain responsible for movement across the outer membrane and periplasmic space; a central domain responsible for receptor recognition; and a C-terminal cytotoxic domain responsible for channel formation in the cytoplasmic membrane [PMID: 15519318].

This entry represents the C-terminal cytotoxic domain, which has a globin-like fold with additional helices at either end.

GO terms

Biological Process

GO:0019835 cytolysis
GO:0050829 defense response to Gram-negative bacterium

Molecular Function

No terms assigned in this category.

Cellular Component

GO:0016021 integral component of membrane

Contributing signatures

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