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Updated: Aug 6, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Cellular location of polyamine transport protein PotD in Streptococcus pneumoniae
Pratik Shah1, Mary Marquart, Lisa R Quin
1Department of Microbiology, University of Mississippi Medical Center, Jackson, 39216, USA.
Abstract:
Streptococcus pneumoniae encodes a transporter for polyamines that contributes to virulence in an animal model. The putative polyamine-binding protein, PotD, has an amino-terminal secretory peptide but no other domains known to be involved in anchoring proteins to the surface of Gram-positive bacteria. Cell fractionation and immunoblotting, along with flow cytometry, suggest that PotD is surface-exposed and anchored to the cytoplasmic membrane by a potentially novel mechanism.
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