Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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BON bacterial OsmY and nodulation domain

SMART accession number:	SM00749
Description:
Interpro abstract (IPR014004):	The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins; outside of this group the distribution is more disparate. The OsmY protein is an Escherichia coli 20 kDa outer membrane or periplasmic protein that is expressed in response to a variety of stress conditions, in particular, helping to provide protection against osmotic shock. One hypothesis is that OsmY prevents shrinkage of the cytoplasmic compartment by contacting the phospholipid interfaces surrounding the periplasmic space. The domain architecture of two BON domains alone suggests that these domains contact the surfaces of phospholipids, with each domain contacting a membrane [(PUBMED:12878000)].
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 1264 BON domains in 654 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a BON domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with BON domain is also avaliable.

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• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Yeats C, Bateman A
  • The BON domain: a putative membrane-binding domain.
  • Trends Biochem Sci. 2003; 28: 352-5
  • Display abstract

  • A novel conserved protein region - 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. Functional annotation in the literature suggests that it interacts with phospholipid membranes. A lack of catalytic residues in the sequence alignment supports the hypothesis that it is a binding domain.

• Metabolism (metabolic pathways involving proteins which contain this domain)

• % proteins involved KEGG pathway ID Description 100.00 map03090 Type II secretion system This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with BON domain which could be assigned to a KEGG orthologous group, and not all proteins containing BON domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Links (links to other resources describing this domain)

• INTERPRO	IPR014004

Send comments to Ivica Letunic