The structure, function, and origin of the microcin H47 ATP-binding cassette exporter indicate its relatedness to that of colicin V

Antimicrob Agents Chemother. 2001 Mar;45(3):969-72. doi: 10.1128/AAC.45.3.969-972.2001.

Abstract

Microcin H47, a gene-encoded peptide antibiotic produced by a natural Escherichia coli strain, was shown to be secreted by a three-component ATP-binding cassette exporter which was revealed to be strongly related to that of colicin V. The results of sequence and gene fusion analyses, as well as heterologous complementation assays, are presented.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / genetics*
  • ATP-Binding Cassette Transporters / physiology
  • Amino Acid Sequence
  • Anti-Bacterial Agents
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / physiology
  • Colicins / chemistry
  • DNA, Bacterial / analysis
  • Escherichia coli / genetics*
  • Escherichia coli / physiology
  • Escherichia coli Proteins*
  • Molecular Sequence Data
  • Multigene Family
  • Peptides
  • Restriction Mapping
  • Sequence Homology, Amino Acid

Substances

  • ATP-Binding Cassette Transporters
  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Colicins
  • DNA, Bacterial
  • Escherichia coli Proteins
  • MchE protein, E coli
  • MchF protein, E coli
  • Peptides

Associated data

  • GENBANK/AJ278866