Protein Family Models

The PapC N-terminal domain is a structural domain found at the N-terminus of the E. coli PapC protein. Pili are assembled using the chaperone usher system. In E.coli this is composed of the chaperone PapD and the usher PapC. This domain represents the N-terminal domain from PapC and its homologues. This domain is involved in substrate binding [1]. [1]. 15920478. Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. Nishiyama M, Horst R, Eidam O, Herrmann T, Ignatov O, Vetsch M, Bettendorff P, Jelesarov I, Grutter MG, Wuthrich K, Glockshuber R, Capitani G;. EMBO J. 2005;24:2075-2086. (from Pfam)

Date:

2024-10-16

The PapC C-terminal domain is a structural domain found at the C-terminus of the E. coli PapC protein. Pili are assembled using the chaperone usher system. In E.coli this is composed of the chaperone PapD and the usher PapC. This domain represents the C-terminal domain from PapC and its homologues. This domain has a beta-sandwich structure similar to the plug domain of PapC [1]. [1]. 20118254. Structural homology between the C-terminal domain of the PapC usher and its plug. Ford B, Rego AT, Ragan TJ, Pinkner J, Dodson K, Driscoll PC, Hultgren S, Waksman G;. J Bacteriol. 2010;192:1824-1831. (from Pfam)

Date:

2024-10-16

In Gram-negative bacteria the biogenesis of fimbriae (or pili) requires a two- component assembly and transport system which is composed of a periplasmic chaperone and an outer membrane protein which has been termed a molecular 'usher' [1-3]. The usher protein is rather large (from 86 to 100 Kd) and seems to be mainly composed of membrane-spanning beta-sheets, a structure reminiscent of porins. Although the degree of sequence similarity of these proteins is not very high they share a number of characteristics. One of these is the presence of two pairs of cysteines, the first one located in the N-terminal part and the second at the C-terminal extremity that are probably involved in disulphide bonds. The best conserved region is located in the central part of these proteins [4-5]. [1]. 7909802. Chaperone-assisted self-assembly of pili independent of cellular energy. Jacob-Dubuisson F, Striker R, Hultgren SJ;. J Biol Chem. 1994;269:12447-12455. [2]. 7906265. Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli. Schifferli DM, Alrutz MA;. J Bacteriol. 1994;176:1099-1110. [3]. 7906046. Structural and evolutionary relationships between two families of bacterial extracytoplasmic chaperone proteins which function cooperatively in fimbrial assembly. Van Rosmalen M, Saier MH Jr;. Res Microbiol. 1993;144:507-527. [4]. 19380723. Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Huang Y, Smith BS, Chen LX, Baxter RH, Deisenhofer J;. Proc Natl Acad Sci U S A. 2009;106:7403-7407. [5]. 18485872. Fiber formation across the bacterial. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

fimbrial biogenesis outer membrane usher protein may be involved in the export and/or assembly of fimbrial subunits across the outer membrane

Date:

2017-05-24

Involved in export and assembly of fimbriae subunits LpfA

Gene:

lpfC

Date:

2020-10-26