title: A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli.
abstract: We have purified to homogeneity a 15 kDa-protein from a ribosomal salt extract of Escherichia coli that compensates in vitro a defect of SecA but not of SecB. Removal of this protein from a cell-free transcription/translation system impairs translocation into plasma membrane vesicles of the precursors of LamB and to a lesser degree also of OmpA. These results suggest a role of the 15 kDa-protein in bacterial protein export. The NH2-terminal 35 amino acids were found to be identical to those of the skp (firA) gene product, to which several putative functions have previously been attributed.
authors.affiliation: Institute of Biochemistry, University of Freiburg, FRG.
authors.forename: B M
authors.initials: BM
authors.lastname: Thome
authors.forename: H K
authors.initials: HK
authors.lastname: Hoffschulte
authors.forename: E
authors.initials: E
authors.lastname: Schiltz
authors.forename: M
authors.initials: M
authors.lastname: Müller
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D001692:Biological Transport; D004926:Escherichia coli / Q000378:metabolism*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012995:Solubility
chemical_list: D001426:Bacterial Proteins