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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)
TIGR00156 family protein
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).
YgiW/YdeI family stress tolerance OB fold protein
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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