Affiliation:
1. Department of Cell Physiology, Boston Biomedical Research Institute, Massachusetts 02114.
Abstract
We identified the phosphoglycerate transporter gene of Salmonella typhimurium and its polypeptide product and determined the nucleotide sequence of the gene. The predicted translation product was a protein of 406 amino acid residues and was extremely hydrophobic, a feature that is consistent with its role in membrane transport. Hydropathy analysis suggested that there are eight transmembrane segments of at least 20 amino acid residues for the protein. The transcription start point was mapped to lie at position -44 relative to the putative translational initiation start point. Comparison of PgtP with UhpT and GlpT, the membrane-bound proteins involved in the transport of hexose-6-phosphate and glycerol-3-phosphate, respectively, revealed a very high degree of amino acid sequence similarity among them, reflecting not only similar structures and functions among these polypeptides but also a common evolutionary origin for them.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
39 articles.
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