FAQ

prepilin peptidase activity

OBSOLETE. Catalysis of the cleavage of a Gly-Phe bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1992-2005
01219922005

Papers overview

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2005
2005
Analysis of the pilU gene for the prepilin peptidase involved in the biogenesis of type IV pili encoded by plasmid R64
In many type IV pili, the N-terminal amino acid of the pilin subunit is N-methylated phenylalanine. A prepilin peptidase removes… (More)
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1998
1998
A second prepilin peptidase gene in Escherichia coli K-12.
Escherichia coli K-12 strains grown at 37 degrees C or 42 degrees C, but not at 30 degrees C, process the precursors of the… (More)
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Review
1997
Review
1997
Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria--a review.
The main terminal branch (MTB) of the general secretory pathway is used by a wide variety of Gram- bacteria to transport… (More)
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Review
1994
Review
1994
Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa.
We have described the characterization of a protein initially identified as having an essential function in biogenesis of polar… (More)
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1992
1992
An enzyme with type IV prepilin peptidase activity is required to process components of the general extracellular protein secretion pathway of Klebsiella oxytoca.
The last gene (pulO) of the pulC-O pullulanase secretion gene operon of Klebsiella oxytoca codes for a protein that is 52… (More)
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1992
1992
PulO, a component of the pullulanase secretion pathway of Klebsiella oxytoca, correctly and efficiently processes gonococcal type IV prepilin in Escherichia coli.
The PulO protein required for extracellular secretion of pullulanase by Klebsiella oxytoca is known to be highly homologous to… (More)
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