A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria

T. Dinh, I. T. Paulsen, M. H. Saier*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-review

249 Citations (Scopus)

Abstract

Seventeen fully sequenced and two partially sequenced extracytoplasmic proteins of purple, gram-negative bacteria constitute a homologous family termed the putative membrane fusion protein (MFP) family. Each such protein apparently functions in conjunction with a cytoplasmic membrane transporter of the ATP-binding cassette family, major facilitator superfamily, or heavy metal resistance/nodulation/cell division family to facilitate transport of proteins, peptides, drugs, or carbohydrates across the two membranes of the gram-negative bacterial cell envelope. Evidence suggests that at least some of these transport systems also function in conjunction with a distinct outer membrane protein. We report here that the phylogenies of these proteins correlate with the types of transport systems with which they function as well as with the natures of the substrates transported. Characterization of the MFPs with respect to secondary structure, average hydropathy, and average similarity provides circumstantial evidence as to how they may allow localized fusion of the two gram-negative bacterial cell membranes. The membrane fusion protein of simian virus 5 is shown to exhibit significant sequence similarity to representative bacterial MFPs.

Original languageEnglish
Pages (from-to)3825-3831
Number of pages7
JournalJournal of Bacteriology
Volume176
Issue number13
Publication statusPublished - 1994
Externally publishedYes

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