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PorT is a membrane-associated protein shown to be essential for the maturation and secretion of a class of cysteine proteinases, the gingipains, from the periodontal pathogen Porphyromonas gingivalis. It was previously reported that PorT is located on the periplasmic surface of the inner membrane to function as a chaperone for the maturing proteinases. In a recent report, a theoritical outer-membrane localization model, which suggested that PorT is an integral outer-membrane protein with eight anti-parallel, membrane-traversing ß-strands, was confirmed by the structural and functional tolerance of PorT to hexahistidine (6xHis) tag insertions at selected locations within the protein using site-directed mutagenesis. PorT homologues have been found in restricted members of the Bacteroidetes phylum where there is potential for PorT to participate in the maturation and secretion of proteins with characteristic C-terminal domains (CTDs).
The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis
Mol Microbiol. 2011 Mar;79(5):1380-401. doi: 10.1111/j.1365-2958.2010.07530.x. Epub 2011 Jan 18.
Verification of a topology model of PorT as an integral outer-membrane protein in Porphyromonas gingivalis
Microbiology (Reading). 2009 Feb;155(Pt 2):328-337. doi: 10.1099/mic.0.024323-0.
Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis
J Biol Chem. 2005 Mar 11;280(10):8668-77. doi: 10.1074/jbc.M413544200. Epub 2005 Jan 4.