PROSITE documentation PDOC51694
Peptidase family M66 domain profile


The peptidase family M66 [E1] domain is a zinc metalloprotease found in:

  • Enterohemorrhagic Escherichia coli (EHEC) neutral zinc metalloprotease StcE (EC 3.4.24.-).
  • Aeromonas hydrophila ToxR-regulated lipoprotein TagA.
  • Vibrio cholerae ToxR-activated gene A lipoprotein TagA (EC 3.4.24.-).

The peptidase family M66 domain adopts a characteristic mixed α+β and a conserved Met-turn (see <PDB:3UJZ>), features that place it within the metzincin superfamily of metalloproteases including astacins, ADAMs (a disintegrin and metalloprotease) (see <PDOC50215>) and matrixins. Notably, a central substrate-binding cleft containing the active site separates the peptidase family M66 domain into two subdomains SD1 and SD2. SD1 consists of a twisted β sheet packed on both sides by three helices. A sharp turn introduced by a conserved Gly in the zinc-binding motif along the active site helix then leads to SD2, which, after a series of convoluted loops, terminates in an helix. The peptidase family M66 coordinates an essential zinc ion in the characteristic tetrahedral fashion and possesses the extended zinc-binding motif HExxHxxGxxH [1].

The profile we developed covers the entire peptidase family M66 domain.

Last update:

October 2013 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

PEPTIDASE_M66, PS51694; Peptidase family M66 domain profile  (MATRIX)


1AuthorsYu A.C.Y. Worrall L.J. Strynadka N.C.J.
TitleStructural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection.
SourceStructure 20:707-717(2012).
PubMed ID22483117


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