Literature summary for 3.4.14.11 extracted from

Hafeez, Z.; Cakir-Kiefer, C.; Lecomte, X.; Miclo, L.; Dary-Mourot, A.
The X-prolyl dipeptidyl-peptidase PepX of Streptococcus thermophilus initially described as intracellular is also responsible for peptidase extracellular activity (2019), J. Dairy Sci., 102, 113-123 .

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Organism

Organism	UniProt	Comment	Textmining
Streptococcus thermophilus	Q03J44	-	-
Streptococcus thermophilus LMD-9	Q03J44	-	-

General Information

General Information	Comment	Organism
physiological function	the growth rate of a gene disruption mutant is reduced by a factor of 1.5 and 1.6 in milk and M17 medium supplemented with lactose, respectively. The mutant strain is not able to hydrolize beta-casomorphin-7 present in the medium. No peptide hydrolysis is highlighted in cell-free filtrate of wild-type	Streptococcus thermophilus

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Release 2023.1 (January 2023)