Protein Family Models

VesB is a serine protease that is secreted by the type II secretion system (T2S) in Vibrio cholerae (Swiss:Q9KSQ6). It efficiently cleaves a trypsin substrate, but not chymotrypsin and elastase substrates [1]. It has been suggested to contribute to intestinal growth or pathogenesis, although is not the only factor required for intestinal survival. VesB can cleave the A subunit of cholera toxin, a process important for cholera toxin activation [1]. It consists of a protease domain (Pfam:PF00089) followed by a Ig-like domain, represented in this entry, which may be involved in one or more different functions such as stabilizing the protease domain, co-defining substrate specificity, binding to the bacterial surface and being part of a yet undefined secretion motif of the T2S system [1]. This protein belongs to the chymotrypsin subfamily A (which includes mostly eukaryotic proteases), having a structure and specificity profile resembling that of eukaryotic trypsin-like proteases. This domain is also found in some eukaryotic protein, such as HYDIN and CFA65 from human (which contain repeated Ig-like domains). Paper describing PDB structure 4lk4. [1]. 24459146. Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB. Gadwal S, Korotkov KV, Delarosa JR, Hol WG, Sandkvist M;. J Biol Chem. 2014;289:8288-8298. (from Pfam)

Date:

2025-01-31

These hypothetical proteins, from bacteria such as Rhodopirellula baltica, Bacteroides thetaiotaomicron, and Porphyromonas gingivalis, share a region of conserved sequence towards their N-termini. (from Pfam)

Date:

2025-01-31

DUF1573 domain-containing protein

Date:

2017-12-18