BTLCP proteins: A novel family of bacterial transglutaminase-like cysteine proteinases

Krzysztof Ginalski, Lisa Kinch, Leszek Rychlewski, Nick V. Grishin

Research output: Contribution to journalShort survey

19 Scopus citations

Abstract

Using sequence similarity searches and top-of-the-range fold-recognition methods, we have identified a novel family of bacterial transglutaminase-like cysteine proteinases (BTLCPs) with an invariant Cys-His-Asp catalytic triad and a predicted N-terminal signal sequence. This family of previously uncharacterized hypothetical proteins encompasses sequences of unknown function from DUF920 (in the Pfam database) and COG3672. BTLCPs are predicted to possess the papain-like cysteine proteinase fold and catalyze post-translational protein modification through transamidase, acetylase or hydrolase activity. Inspection of neighboring genes encoding BTLCPs suggests a link between this predicted activity and a type-I secretion system resembling ATP-binding cassette exporters of toxins and proteases involved in bacterial pathogenicity.

Original languageEnglish (US)
Pages (from-to)392-395
Number of pages4
JournalTrends in Biochemical Sciences
Volume29
Issue number8
DOIs
StatePublished - Aug 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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