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Bacterial OB fold (BOF) protein
Proteins in this family form an OB-fold. Analysis of the predicted binding site of BOF family proteins implies that they lack nucleic acid-binding properties [1]. They contain an predicted N-terminal signal peptide which indicates that they localise in the periplasm where they may function to bind proteins, small molecules, or other typical OB-fold ligands [1]. As hypothesised for the distantly related OB-fold containing bacterial enterotoxins, the loss of nucleotide-binding function and the rapid evolution of the BOF ligand-binding site may be associated with the presence of BOF proteins in mobile genetic elements and their potential role in bacterial pathogenicity [1]. [1]. 15178340. BOF: a novel family of bacterial OB-fold proteins.. Ginalski K, Kinch L, Rychlewski L, Grishin NV;. FEBS Lett. 2004;567:297-301. (from Pfam)
YgiW/YdeI family stress tolerance OB fold protein
YgiW/YdeI family stress tolerance OB fold protein may function to bind proteins, small molecules, or other typical OB-fold ligands
NirD/YgiW/YdeI family stress tolerance protein
Members of this family possess an N-terminal signal peptide, and are associated with tolerance to various toxic stresses. These include antimicrobial peptides (YdeI), hydrogen peroxide (YgiW and YdeI), and nickel (NcrY and NirD).
This HMM describes certain OB fold proteins involved in stress tolerance, including YgiW and YdeI , both of which are found in both Escherichia coli and Salmonella enterica, as well as more broadly.
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