Protein Family Models

This domain was initially identified from proteins from C. hutchinsonii giving rise to the CHU name. This domain adopts an immunoglobulin like domain that is foundat the C-terminus of various bacterial cell surface proteins. This domain was shown to be essential for localisation of the CHU_3220 protein. It is likely that this domain target the proteins containing it to the type IX secretion system. This domain is cleaved off the protein which is then anchored to the outer membrane [2]. [1]. 27742681. Identification and Characterization of a Large Protein Essential for Degradation of the Crystalline Region of Cellulose by Cytophaga hutchinsonii. Wang S, Zhao D, Bai X, Zhang W, Lu X;. Appl Environ Microbiol. 2016; [Epub ahead of print]. [2]. 28714554. Type IX secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers. Veith PD, Glew MD, Gorasia DG, Reynolds EC;. Mol Microbiol. 2017;106:35-53. (from Pfam)

Date:

2024-10-16

This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion [1]. [1]. 10933504. HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold. Callebaut I, Gilges D, Vigon I, Mornon JP;. Protein Sci 2000;9:1382-1390. (from Pfam)

Date:

2024-10-16

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 TIGR04131, recognized as sorting signal by T9SS, is now known as type B, and is quite distinct from type A (see TIGR04183). 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:

2023-07-12