Protein Family Models

Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease [2]. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold. [1]. 24007199. Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment. Veith PD, Nor Muhammad NA, Dashper SG, Likic VA, Gorasia DG, Chen D, Byrne SJ, Catmull DV, Reynolds EC;. J Proteome Res. 2013;12:4449-4461. [2]. 22593568. PG0026 is the C-terminal signal peptidase of a novel secretion system of Porphyromonas gingivalis. Glew MD, Veith PD, Peng B, Chen YY, Gorasia DG, Yang Q, Slakeski N, Chen D, Moore C, Crawford S, Reynolds EC;. J Biol Chem. 2012;287:24605-24617. (from Pfam)

Date:

2024-10-16

This HMM described a domain that is often repeated in pilins such as SpaA, and that often forms isopeptide bonds cross-linking amino acid side chains, giving the pilins added strength.

Date:

2024-10-16

Date:

2024-08-14

This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with Pfam:PF07715 and Pfam:PF00593. [1]. 10986238. Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron. Shipman JA, Berleman JE, Salyers AA;. J Bacteriol. 2000;182:5365-5372. [2]. 11717282. Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron. Cho KH, Salyers AA;. J Bacteriol 2001;183:7224-7230. (from Pfam)

Date:

2024-10-16

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

Type IX secretions systems (T9SS) occur in the Bacteroidetes, such as Cytophaga hutchinsonii and Flavobacterium johnsoniae, and are required for the type of gliding motility seen in that lineage, although they are not limited processing target proteins from that system. The C-terminal domain described by TIGR04183, recognized as sorting signal by T9SS, is now known as type A, and is quite distinct from type B (see TIGR04131). Most targets of T9SS are cleaved by a transpeptidase and then attached to a component of the outer membrane, but a few are released in soluble form.

Date:

2023-07-13