{PDOC51694}
{PS51694; PEPTIDASE_M66}
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* Peptidase family M66 domain profile *
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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 alpha+beta 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 beta  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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2013 / First entry.

[ 1] Yu A.C.Y., Worrall L.J., Strynadka N.C.J.
     "Structural insight into the bacterial mucinase StcE essential to
     adhesion and immune evasion during enterohemorrhagic E. coli
     infection."
     Structure 20:707-717(2012).
     PubMed=22483117; DOI=10.1016/j.str.2012.02.015
[E1] https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=M66

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