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Immunoglobulin-like domain BIg-containing protein
This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) Pfam:PF05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor [1]. [1]. 28370712. Structure of the Y. pseudotuberculosis adhesin InvasinE. Sadana P, Monnich M, Unverzagt C, Scrima A;. Protein Sci. 2017;26:1182-1195. (from Pfam)
adhesion domain-containing protein
This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 Pfam:PF05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain [1]. [1]. 28370712. Structure of the Y. pseudotuberculosis adhesin InvasinE. Sadana P, Monnich M, Unverzagt C, Scrima A;. Protein Sci. 2017;26:1182-1195. (from Pfam)
DUF823/DUF824 repeat adhesin RatA
RatA, encoded in a Salmonella pathogenicity island next to its homolog RatB, is a long protein consisting almost entirely of repeats of a DUF823/DUF824 pair (see PF05689 and PF05688, respectively). The DUF823 is also found in the inverse autotransporter adhesin/invasin, where it is called an adhesion domain. DUF824 has now been reclassified as a Bacterial Immunoglobulin-like domain, BIg21.
outer membrane protein RatA
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