Cellular location of polyamine transport protein PotD in Streptococcus pneumoniae.
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.
Shah
Pratik
P
Department of Microbiology, University of Mississippi Medical Center, Jackson, 39216, USA.
Marquart
Mary
M
Quin
Lisa R
LR
Swiatlo
Edwin
E
D000907:Antibodies, Bacterial / Q000276:immunology; D016667:Bacterial Capsules / Q000737:chemistry; D001426:Bacterial Proteins / Q000032:analysis / Q000737:chemistry / Q000276:immunology; D002458:Cell Fractionation; D002462:Cell Membrane / Q000737:chemistry*; D005434:Flow Cytometry; D015151:Immunoblotting; D026901:Membrane Transport Proteins / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D011073:Polyamines / Q000378:metabolism*; D021382:Protein Sorting Signals; D017434:Protein Structure, Tertiary; D013296:Streptococcus pneumoniae / Q000737:chemistry*
D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D011073:Polyamines; D021382:Protein Sorting Signals