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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 PDOC50914
BON domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC50914

Description

The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an α/β predicted fold. There is a conserved glycine residue and several hydrophobic regions. The BON domain can be found in one or more copies and associated with other domains, such as CBS, LysM or FHA (see <PDOC50006>). The BON domain is likely to be a phospholipid-binding domain that is involved in osmotic-shock protection and other cell-membrane-localized processes [1].

The profile we developed covers the entire BON domain.

Last update:

August 2003 / First entry.

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Technical section

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

BON, PS50914; BON domain profile  (MATRIX)


Reference

1AuthorsYeats C. Bateman A.
TitleThe BON domain: a putative membrane-binding domain.
SourceTrends Biochem. Sci. 28:352-355(2003).
PubMed ID12878000



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