Protein Family Models

This entry represents a short repeat found near the C-terminus of some RTX toxins such as Swiss:Q9KS12 [1]. AlphaFold models suggest this repeat forms a beta solenoid structure. These repeats contain a GXGXD motif in each repeat which is similar to that found in the RTX calcium-binding nonapeptide repeat Pfam:PF00353. This suggests that these repeats may also be needed for translocation via the type I secretion system [1]. [1]. 17646359. MARTX, multifunctional autoprocessing repeats-in-toxin toxins. Satchell KJ;. Infect Immun. 2007;75:5079-5084. [2]. 27058787. Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P;. Mol Cell. 2016;62:47-62. (from Pfam)

Date:

2024-10-16

This domain is found in Vibrio cholerae RtxA toxin and VgrG1 protein. This domain cross-links to G-actin leading to cytoskeletal changes [1]. [1]. 22898822. Crystal structure of the VgrG1 actin cross-linking domain of the Vibrio cholerae type VI secretion system. Durand E, Derrez E, Audoly G, Spinelli S, Ortiz-Lombardia M, Raoult D, Cascales E, Cambillau C;. J Biol Chem. 2012;287:38190-38199. (from Pfam)

Date:

2024-10-16

This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with Pfam:PF00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2. (from Pfam)

Date:

2024-08-14

This is a membrane localization domain found in multiple families of bacterial toxins including all of the clostridial glucosyltransferase toxins and various MARTX toxins (multifunctional-autoprocessing RTX toxins) [1,4]. In the Pasteurella multocida toxin (PMT) C-terminal fragment, structural analysis have indicated that the C1 domain possesses a signal that leads the toxin to the cell membrane. Furthermore, the C1 domain was found to structurally resemble the phospholipid-binding domain of C. difficile toxin B [2]. Functional studies in Vibrio cholera indicate that the subdomain at the N terminus of RID (Rho-inactivation domain), homologous to the membrane targeting C1 domain of Pasteurella multocida toxin, is a conserved membrane localization domain essential for proper localization [1]. The Rho-inactivation domain (RID) of MARTX (Multifunctional Autoprocessing RTX toxin) is responsible for inactivating the Rho-family of small GTPases in Vibrio cholerae. It is a bacterial toxin that self-process by a cysteine peptidase mechanism [3]. The Vibrio cholerae RTX toxin is an autoprocessing cysteine protease whose activity is stimulated by the intracellular environment [3]. This cysteine peptidase belongs to MEROPS peptidase family G6. [1]. 20212166. Identification of a conserved membrane localization domain within numerous large bacterial protein toxins. Geissler B, Tungekar R, Satchell KJ;. Proc Natl Acad Sci U S A. 2010;107:5581-5586. [2]. 17360394. Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin. Kitadokoro K, Kamitani S, Miyazawa M, Hanajima-Ozawa M,. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family belongs to cysteine peptidase family C80. [1]. 18845756. Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain. Lupardus PJ, Shen A, Bogyo M, Garcia KC;. Science. 2008;322:265-268. (from Pfam)

Date:

2024-10-16

This short repeat is found in the RtxA toxin family [1]. [1]. 9927695. Identification of a vibrio cholerae RTX toxin gene cluster that is tightly linked to the cholera toxin prophage. Lin W, Fullner KJ, Clayton R, Sexton JA, Rogers MB, Calia KE, Calderwood SB, Fraser C, Mekalanos JJ;. Proc Natl Acad Sci U S A 1999;96:1071-1076. (from Pfam)

Date:

2024-10-16

This catalytic domain is found in a very wide range of enzymes. [1]. 1409539. The alpha/beta hydrolase fold. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A;. Protein Eng 1992;5:197-211. (from Pfam)

Date:

2024-10-16