CPDadh: A new peptidase family homologous to the cysteine protease domain in bacterial MARTX toxins

Jimin Pei, Patrick J. Lupardus, K. Christopher Garcia, Nick V. Grishin

Research output: Contribution to journalArticle

6 Scopus citations


A cysteine protease domain (CPD) has been recently discovered in a group of multifunctional, autoprocessing RTX toxins (MARTX) and Clostridium difficile toxins A and B. These CPDs (referred to as CPDmartx) autocleave the toxins to release domains with toxic effects inside host cells. We report identification and computational analysis of CPDadh. a new cysteine peptidase family homologous to CPDmartx. CPDadh and CPDmartx share a Rossmann-like structural core and conserved catalytic residues. In bacteria, domains of the CPDadh family are present at the N-termini of a diverse group of putative cell-cell interaction proteins and at the C-termini of some RHS (recombination hot spot) proteins. In eukaryotes, catalytically inactive members of the CPDadh family are found in cell surface protein NELF (nasal embryonic LHRH factor) and some putative signaling proteins. Published by Wiley-Blackwell.

Original languageEnglish (US)
Pages (from-to)856-862
Number of pages7
JournalProtein Science
Issue number4
StatePublished - Apr 2009



  • Cell adhesion molecules
  • Cysteine protease domain
  • Multifunctional autoprocessing RTX toxins
  • Nasal embryonic LHRH factor
  • RHS proteins
  • Repeats-in-toxin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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