Protein Family Models

This entry represents the autochaperone domain of type 1 (AC-1) in the Type Va Secretion System (T5aSS). Autotransporters (ATs) belong to a family of modular proteins secreted by the Type V, subtype a, secretion system (T5aSS) and considered as an important source of virulence factors in lipopolysaccharidic diderm bacteria (archetypical Gram-negative bacteria). The AC of type 1 with beta-fold appears as a prevalent and conserved structural element exclusively associated to beta-helical AT passenger [1]. [1]. 29375499. Identification of the Autochaperone Domain in the Type Va Secretion System (T5aSS): Prevalent Feature of Autotransporters with a beta-Helical Passenger. Rojas-Lopez M, Zorgani MA, Kelley LA, Bailly X, Kajava AV, Henderson IR, Polticelli F, Pizza M, Rosini R, Desvaux M;. Front Microbiol. 2018;8:2607. (from Pfam)

Date:

2024-10-16

ESPR (Extended Signal Peptide Region) is found in type V secretion system (T5SS) system proteins. Many such proteins are virulence factors, such autotransporter adhesins YapH (Yersinia pestis), FdeC (Escherhical coli), and BapA (Bartonella henselae), and autotransporter toxins such as VacA (Helicobacter pylori), SepA (Shigella flexneri), and Vat (Escherichia coli).

Date:

2024-10-16

The AIDA repeat is found on bacterial autotransporter proteins. As the repeat is short and occurs multiple times, it is likely to be the region of the transporter that acts as the stalk between the beta-barrel inserted into the membrane and the N-terminal head domain. [1]. 15547278. Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation. Sherlock O, Schembri MA, Reisner A, Klemm P;. J Bacteriol. 2004;186:8058-8065. [2]. 15950405. Characterization and immuno-detection of AIDA-I adhesin isolated from porcine Escherichia coli. Fang Y, Ngeleka M, Middleton DM, Simko E;. Vet Microbiol. 2005;109:65-73. [3]. 1625582. AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule. Benz I, Schmidt MA;. Mol Microbiol. 1992;6:1539-1546. [4]. 22466966. Discovery of an archetypal protein transport system in bacterial outer membranes. Selkrig J, Mosbahi K, Webb CT, Belousoff MJ, Perry AJ, Wells TJ, Morris F, Leyton DL, Totsika M, Phan MD, Celik N, Kelly M, Oates C, Hartland EL, Robins-Browne RM, Ramarathinam SH, Purcell AW, Schembri MA, Strugnell RA, Henderson IR, Walker D, Lithgow T;. Nat Struct Mol Biol. 2012;19:506-510. [5]. 15123066. Bugs and the gut: an unstable marriage. Farthing MJ;. Best Pract Res Clin Gastroenterol. 2004;18:233-239. (from Pfam)

Date:

2024-10-16

This model describes two tandem copies of a strand-loop-strand repeat that occurs often in type V secretion system (T5SS). These repeats usually occur in the passenger domain of the classical monomeric autotransporter. Proteins with this repeat often are encoded next to a member of family TIGR04414, the Aah/TibC family O-heptosyltransferase, and may be glycosylated in regions with this repeat.

Date:

2020-10-23

Members of this family, restricted to Escherichia coli (including E. coli K-12) are the autotransporter adhesin Ag43 (antigen 43), also known as flu, or its calcium-binding homolog Cah, differing mostly in the central region. The C-terminal region forms an outer membrane beta-barrel autotransporter domain, which enables type V secretion (autotransport).

Date:

2021-02-08