Literature summary for 3.4.21.107 extracted from

Israeli, M.; Elia, U.; Rotem, S.; Cohen, H.; Tidhar, A.; Bercovich-Kinori, A.; Cohen, O.; Chitlaru, T.
Distinct contribution of the HtrA protease and PDZ domains to its function in stress resilience and virulence of Bacillus anthracis (2019), Front. Microbiol., 10, 255 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus anthracis

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of a truncated variant lacking the PDZ domain. Variant is abundantly secreted and processed	Bacillus anthracis
S255A	mutation of the catalytic serine residue. Mutant protein does not undergo autolysis and much more abundant in the cellular fraction and almost undetected in its secreted form	Bacillus anthracis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Bacillus anthracis	-	-

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	A0A2B6C4K2	-	-

General Information

General Information	Comment	Organism
physiological function	the proteolytic activity of HtrA is essential for its N-terminal autolysis and subsequent release into the extracellular milieu, while the PDZ domain is dispensable for this process. The PDZ domain appears to be dispensable for most of the functions related to stress resilience as well as involvement of HtrA in assembly of the bacterial S-layer. The proteolytic activity, but not the PDZ domain, appears to be dispensable for the role of HtrA in mediating upregulation of the extracellular protease NprA under starvation stress. In a murine model of anthrax, the HtrA PDZ domain is dispensable for manifestation of Bacillus anthracis virulence	Bacillus anthracis

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Release 2023.1 (January 2023)