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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00249
Channel forming colicins signature


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00249

Description

Colicins are plasmid-encoded polypeptide toxins produced by and active against Escherichia coli and closely related bacteria. The channel-forming colicins are transmembrane proteins that depolarize the cytoplasmic membrane, leading to dissipation of cellular energy [1,2]. Colicins A, B, E1, Ia, Ib, and N belong to that group. The N-terminal part of these colicins is involved in their uptake; the central part is important for binding to outer membrane receptors and the C-terminal part is the channel-forming region.

As a signature for this type of colicins, we have selected one of the most conserved region of the channel-forming domain.

Last update:

November 1990 / Text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CHANNEL_COLICIN, PS00276; Channel forming colicins signature  (PATTERN)


References

1AuthorsPattus F. Massotte D. Wilmsen H.U. Lakey J. Tsernoglou D. Tucker A. Parker M.W.
TitleColicins: prokaryotic killer-pores.
SourceExperientia 46:180-192(1990).
PubMed ID1689257

2AuthorsCramer W.A. Cohen F.S. Merrill A.R. Song H.Y.
TitleStructure and dynamics of the colicin E1 channel.
SourceMol. Microbiol. 4:519-526(1990).
PubMed ID1693745



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