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Sbs-2, a secreted peptidoglycan hydrolase produced by Shiga toxin-producing Escherichia coli O99, has been shown previously to be an enteropathogenic toxin and an important virulence factor for the Shiga toxin E. coli O157:H7. A functional E. coli O99 Sbs-2 was partially purified from a culture of S. flexneri. The Sbs-2 activity produced by E. coli O99 had a molecular weight of about 50 kDa and activity against glycan substrates of the Bacteroides fragilis group. This Sbs-2 was shown to be a multifunctional protein and in addition to its peptidoglycan glycanase activity, it was also able to degrade mannosylated proteins, muramidase, phosphatase and DNA. The functional E. coli O99 Sbs-2 protein was found to be identical to the precursor of the Shiga toxin, which is cleaved to the amino-terminus by the bacterial sortase to form the toxic portion of the toxin. The peptidoglycan hydrolase activity of the E. coli O99 Sbs-2 protein does not appear to be the only mechanism used by this S.