The AprX protein of Pseudomonas aeruginosa: a new substrate for the Apr type I secretion system

Gene. 2001 Jan 10;262(1-2):147-53. doi: 10.1016/s0378-1119(00)00541-2.

Abstract

Protein secretion in Pseudomonas aeruginosa involves different mechanisms. The type II and type III secretory pathways control the extracellular release of a wide range of substrates. The type I secretion process, or ABC transporter, was believed to be exclusively involved in alkaline protease secretion. Recently, it was discovered that a P. aeruginosa heme binding protein, HasAp, is also secreted by a type I process. We present here the identification of a third putative type I-dependent protein of P. aeruginosa, AprX. The function of this protein has not yet been elucidated but very interestingly it appears to be linked to the apr cluster, and organized in one single operon together with the aprD, -E and -F genes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters*
  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Escherichia coli / genetics
  • Gene Order
  • Membrane Proteins*
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Operon
  • Pseudomonas aeruginosa / genetics
  • Pseudomonas aeruginosa / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / genetics*
  • Serine Endopeptidases / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • AprD protein, Pseudomonas fluorescens
  • AprE protein, Bacteria
  • AprF protein, Pseudomonas
  • Bacterial Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • Recombinant Proteins
  • AprX protein, bacteria
  • Serine Endopeptidases