Protein Family Models

This domain is found on peptidase C25 proteins and has no known function. (from Pfam)

Date:

2024-08-14

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. [1]. 20233299. STRUCTURE DETERMINATION AND ANALYSIS OF A HEMOLYTIC GINGIPAIN ADHESIN DOMAIN FROM PORPHYROMONAS GINGIVALIS. Li N, Yun P, Nadkarni MA, Ghadikolaee NB, Nguyen KA, Lee M, Hunter N, Collyer CA;. Mol Microbiol. 2010; [Epub ahead of print]. [2]. 7836351. Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Bios. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This is found at the N terminal end of some of the members of the C25 peptidase family (PF01364). Little is known about the function of this motif. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Date:

2024-08-14

The choice-of-anchor J domain, about 160 amino acids long, occurs as many as times in a protein, although most often only once. Proteins with the domain include proteins with serine hydrolase, metallohydrolase, or adhesin-associated domains. Notably, many members are also found with either the PEP-CTERM term domain, or the type IX secretion system type A domain, both associated with protein-sorting system expected to leave target proteins covalently attached to the bacterial outer membrane.

Date:

2020-10-26

Gene:

rgpA

Date:

2018-07-31