HtrA, also known as DegP and probably identical to the Do protease, is
a heat shock-induced serine protease that is active in the periplasm
of Escherichia coli, Homologues of HtrA have been described in a wide
range of bacteria and in eukaryotes. Its chief role is to degrade misf
olded proteins in the periplasm, Substrate recognition probably involv
es the recently described PDZ domains in the C-terminal half of HtrA a
nd, we suspect, has much in common with the substrate recognition syst
em of the tail-specific protease, Prc (which also possesses a PDZ doma
in). The expression of htrA is regulated by a complex set of signal tr
ansduction pathways, which includes an alternative sigma factor, RpoE,
an anti-sigma factor, RseA, a two-component regulatory system, CpxRA,
and two phosphoprotein phosphatases, PrpA and PrpB. Mutations in the
htrA genes of Salmonella, Brucella and Yersinia cause decreased surviv
al in mice and/or macrophages, and htrA mutants can act as vaccines, a
s cloning hosts and as carriers of heterologous antigens.