This is a family of bacterial protein modules thought to function in various roles including cell adhesion, cell lysis and carbohydrate binding [1]. A tandem repeat of these modules (either two or three repeats) constitute the haemagglutinin/adhesin ...
This is a family of bacterial protein modules thought to function in various roles including cell adhesion, cell lysis and carbohydrate binding [1]. A tandem repeat of these modules (either two or three repeats) constitute the haemagglutinin/adhesin (HA) regions of the gingipains, RgpA, Swiss:Q51816 and Kgp, Swiss:P72194 and Swiss:P72197 [3] expressed by Porphyromonas gingivalis (Bacteroides gingivalis) [2]. They form components of the major extracellular virulence complex RgpA-Kgp - a mixture of proteinases and adhesin domains [4]. The adhesin domains in this complex are found in proteinase-cleaved forms when isolated from the cell surface [5]. Haemagglutinin genes of P. gingivalis [6] (hagA1 HAGA1_PORGI - Swiss:P59915 - and hagA2 HAGA2_PORGI - Swiss:Q51845) suggest that such proteins are composed of eight to ten tandem repeats of these adhesin modules [1]. Genomic data predicts that homologous protein modules are also expressed by a number of other bacteria and form part of putative multi-domain proteins, eg. Swiss:Q26BR9 and Swiss:B0VGL6. These domains may be acting in concert with other adhesion modules thought to be part of these multi-domain proteins such as fibronectin type III, Pfam:PF00041, and Meprin, A5, mu (MAM), Pfam:PF00629, domains.
