Literature summary for 3.4.21.107 extracted from

Cole, J.N.; Aquilina, J.A.; Hains, P.G.; Henningham, A.; Sriprakash, K.S.; Caparon, M.G.; Nizet, V.; Kotb, M.; Cordwell, S.J.; Djordjevic, S.P.; Walker, M.J.
Role of group A Streptococcus HtrA in the maturation of SpeB protease (2007), Proteomics, 7, 4488-4498.

Search for more literature for 3.4.21.107

Cloned(Commentary)

Cloned (Comment)	Organism
gene htrA, DNA and amino acid sequence determination and analysis	Streptococcus pyogenes

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of the deletion mutant HSC5DELTAhtrA	Streptococcus pyogenes

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Streptococcus pyogenes	HtrA is essential for the maturation of cysteine protease streptococcal pyrogenic exotoxin B, SpeB, but is unable to directly process SpeB zymogen, proSpeB to the active form in vitro, thus playing an indirect role in the maturation, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pyogenes	-	a group A Streptococcus species, HSC5, M5 serotyp, gene htrA	-

Reaction

Reaction	Comment	Organism	Reaction ID
acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-/-Val	the trypsin-like serine protease catalytic triad formed by His129, Asp158, and Ser240	Streptococcus pyogenes	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	HtrA is essential for the maturation of cysteine protease streptococcal pyrogenic exotoxin B, SpeB, but is unable to directly process SpeB zymogen, proSpeB to the active form in vitro, thus playing an indirect role in the maturation, overview	Streptococcus pyogenes	?	-	?

Subunits

Subunits	Comment	Organism
More	HtrA contains a putative N-terminal membrane anchor domain, Ile13 to Ile26, a trypsin-like serine protease catalytic triad formed by His129, Asp158, and Ser240, and a single C-terminal PDZ domain, Gly296 to Arg385	Streptococcus pyogenes

Synonyms

Synonyms	Comment	Organism
DegP	-	Streptococcus pyogenes
high-temperature requirement A	-	Streptococcus pyogenes
HtrA	-	Streptococcus pyogenes

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Streptococcus pyogenes

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Streptococcus pyogenes

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Release 2023.1 (January 2023)