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The HtrA family of serine proteases
Author(s) -
Pallen Mark J.,
Wren Brendan W.
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.5601928.x
Subject(s) - periplasmic space , biology , proteases , pdz domain , serine protease , microbiology and biotechnology , escherichia coli , serine , signal transducing adaptor protein , mutant , signal peptide , protease , signal transduction , biochemistry , peptide sequence , phosphorylation , gene , enzyme
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 misfolded proteins in the periplasm. Substrate recognition probably involves the recently described PDZ domains in the C‐terminal half of HtrA and, we suspect, has much in common with the substrate recognition system of the tail‐specific protease, Prc (which also possesses a PDZ domain). The expression of htrA is regulated by a complex set of signal transduction 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 survival in mice and/or macrophages, and htrA mutants can act as vaccines, as cloning hosts and as carriers of heterologous antigens.