Protein Family Models

This entry includes Flagellar hook-associated protein 1 (FlgK or HAP1), one of three HAPs that form the hook-filament junction and has structural similarity to flagellin. FlgK is required for normal flagellum assembly. Proteins in this entry have a multidomain fold comprising an elongated alpha-helical scaffold core, and depending on the bacterial species, a variable number of smaller domains [1]. This entry represents a beta-sandwich domain from FlgK proteins; Salmonella typhimurium FlgK (Swiss:P0A1J5) has one beta-sandwich domain, while FlgK from Burkholderia pseudomallei has two of them protruding from the alpha-helical core, referred to as D2 and D3 domains in [1], of which the first one, D2, is covered in this entry [1]. FlgK has cytotoxic effects suggesting an important role in pathogenesis and is highly immunogenic. Domains D2 and D3 from B. pseudomallei have been identified as epitopes with increased immunogenic potential for vaccine development. Paper describing PDB structure 4ut1. [1]. 25645451. From crystal structure to in silico epitope discovery in the Burkholderia pseudomallei flagellar hook-associated protein FlgK. Gourlay LJ, Thomas RJ, Peri C, Conchillo-Sole O, Ferrer-Navarro M, Nithichanon A, Vila J, Daura X, Lertmemongkolchai G, Titball R, Colombo G, Bolognesi M;. FEBS J. 2015;282:1319-1333. (from Pfam)

Date:

2024-10-16

This entry represents a mainly helical domain found in flagellar hook-associated protein FlgK and related proteins. FlgK is one of three hook associated proteins that form the hook-filament junction. This domain adopts a broken antiparallel helical bundle comprising six helical segments [1-2]. Paper describing PDB structure 4ut1. [1]. 25645451. From crystal structure to in silico epitope discovery in the Burkholderia pseudomallei flagellar hook-associated protein FlgK. Gourlay LJ, Thomas RJ, Peri C, Conchillo-Sole O, Ferrer-Navarro M, Nithichanon A, Vila J, Daura X, Lertmemongkolchai G, Titball R, Colombo G, Bolognesi M;. FEBS J. 2015;282:1319-1333. Paper describing PDB structure 5xbj. [2]. 29147015. Structure of FlgK reveals the divergence of the bacterial Hook-Filament Junction of Campylobacter. Bulieris PV, Shaikh NH, Freddolino PL, Samatey FA;. Sci Rep. 2017;7:15743. (from Pfam)

Date:

2024-10-29

This family consists of a number of C-terminal domains of unknown function. This domain seems to be specific to flagellar basal-body rod and flagellar hook proteins in which Pfam:PF00460 is often present at the extreme N terminus. [1]. 2129540. FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium. Homma M, Kutsukake K, Hasebe M, Iino T, Macnab RM;. J Mol Biol. 1990;211:465-477. (from Pfam)

Date:

2024-10-16

flagellar hook-associated protein FlgK forms the junction between the hook and the filament in the flagellum together with FlgL and provides a structural base where flagellin, a filament-forming protein, is inserted for the initiation of filament elongation

Date:

2019-06-24

The flagellar hook-associated protein FlgK of bacterial flagella has conserved N- and C-terminal domains. The central region is highly variable in length and sequence, and often contains substantial runs of low-complexity sequence. This model is built from an alignment of FlgK sequences with the central region excised. Note that several other proteins of the flagellar apparatus also are homologous in the N- and C-terminal regions to FlgK, but are excluded from this model.

Gene:

flgK

Date:

2024-06-24