Protein Family Models

This is C-terminal domain (CTD) of M60-peptidases Pfam:PF13402 [1]. It Can also be found at the C-terminal region of gingipain B (RgpB) from P. gingivalis. It was found to possess a typical Ig-like fold encompassing seven antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that can spontaneously dimerise through C-terminal strand swapping. Translocation of gingipains from the periplasm across the OM is dependent on the conserved CTD, which appears to be important for secretion of the proteins and in particular, truncation of the last few C-terminal residues of this domain leads to accumulation of gingipains in the periplasm. Subsequently, the T9SS targeting signal was demonstrated to reside within the last 22 residues at the C-terminus of the CTD. During gingipain translocation across the OM, the CTD is cleaved off by PorU [2]. [1]. 28096352. Recognition of protein-linked glycans as a determinant of peptidase activity. Noach I, Ficko-Blean E, Pluvinage B, Stuart C, Jenkins ML, Brochu D, Buenbrazo N, Wakarchuk W, Burke JE, Gilbert M, Boraston AB;. Proc Natl Acad Sci U S A. 2017;114:E679. [2]. 27005013. The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal beta-sandwich domain. de Diego I, Ksiazek M, Mizgalska D, Koneru L, Golik P, Szmigielski B, Nowak M, Nowakowska Z, Potempa B, Houston JA, Enghild JJ, Thogersen IB, Gao J, Kwan AH, Trewhella J, Dubin G, Gomis-Ruth FX, Nguyen KA, Potempa J;. Sci Rep. 2016;6:23123. (from Pfam)

Date:

2024-10-16

This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity [1]. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut [1,2]. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function [2]. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonisation of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes [3]. This family has been augmented by a merge with the sequences in the Enhancin Pfam family. [1]. 9192677. An intestinal mucin is the target substrate for a baculovirus enhancin. Wang P, Granados RR;. Proc Natl Acad Sci U S A 1997;94:6977-6982. [2]. 16081094. Comparison of the bacterial Enhancin-like proteins from Yersinia and Bacillus spp. with a baculovirus Enhancin. Galloway CS, Wang P, Winstanley D, Jones IM;. J Invertebr Pathol. 2005;90:134-137. [3]. 22299034. A novel extracellular metallopeptidase domain shared by animal host-associated mutualistic and pathogenic microbes. Nakjang S, Ndeh DA, Wipat A, Bolam DN, Hirt RP;. PLoS One. 2012;7:e30287. (from Pfam)

Date:

2024-10-16

This domain is also known as the discoidin (DS) domain family [1]. Extension of family to prokaryotes. [1]. 9684896. The discoidin domain family revisited: new members from prokaryotes and a homology-based fold prediction. Baumgartner S, Hofmann K, Chiquet-Ehrismann R, Bucher P;. Protein Sci 1998;7:1626-1631. (from Pfam)

Date:

2024-10-16