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Peptidase family M34 includes the C-terminal catalytic domain of anthrax lethal factor (ATLF), the protective antigen-binding domains of ATLF and edema factor, and Pro-Pro endopeptidase Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA. EF is comprised of the PABD and an adenylyl cyclase domain. This family also includes Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) which is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",