PROSITE documentation PDOC51694Peptidase 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.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Yu A.C.Y. Worrall L.J. Strynadka N.C.J. |
Title | Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. | |
Source | Structure 20:707-717(2012). | |
PubMed ID | 22483117 | |
DOI | 10.1016/j.str.2012.02.015 |
E1 | Title | https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=M66 |
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