Protein Family Models

This entry is composed of PKD domains found in bacterial surface proteins. (from Pfam)

Date:

2024-08-14

Immune inhibitor A(InhA)-type metallopeptidases are potential virulence factors secreted by members of the Bacillus cereus group (BCG) and belong to the thuringilysin family within the metzincin clan of metallopeptidases, M6 in the MEROPS database. The structure of these proteins consists of four domains: a pro-peptide, a catalytic domain, a domain reminiscent of viral envelope glycoproteins (VEG), and a MAM domain grafted into the latter [1]. This entry represents the VEG domain found at the C-terminal of InhA and PrtV peptidases (a slightly more distant thuringilysin family members). It consists of a central parallel beta-sandwich comprised by an upper five-stranded mixed sheet and a lower four-stranded antiparallel sheet [1]. [1]. 26745529. Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome. Arolas JL, Goulas T, Pomerantsev AP, Leppla SH, Gomis-Ruth FX;. Structure. 2016;24:25-36. (from Pfam)

Date:

2024-10-16

Immune inhibitor A (InhA)-type metallopeptidases are potential virulence factors secreted by members of the Bacillus cereus group (BGC) and belong to the thuringilysin family within the metzincin clan of metallopeptidases, M6 in the MEROPS database. The structure revealed four domains: a pro-peptide, a catalytic domain, a domain reminiscent of viral envelope glycoproteins (VEG) and a MAM domain grafted into the latter [1]. This entry represents the MAM domain found in InhA and PrtV peptidases from Vibrio (a slightly more distant thuringilysin family members), which is required for proper protein expression and has certain flexibility. It is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets, grafted between the second and third strands of the upper sheet of VEG [1]. This domain displays closest structural similarity with MAM domains such as the one from the human MP, meprin beta. [1]. 26745529. Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome. Arolas JL, Goulas T, Pomerantsev AP, Leppla SH, Gomis-Ruth FX;. Structure. 2016;24:25-36. (from Pfam)

Date:

2024-10-16

The insect pathogenic Gram-positive Bacillus thuringiensis secretes immune inhibitor A, a metallopeptidase, which specifically cleaves host antibacterial proteins. A homologue of immune inhibitor A, PrtV, has been identified in the Gram-negative human pathogen Vibrio cholerae [4]. The structure revealed four domains: a pro-peptide, a catalytic domain (represented in this entry), a domain reminiscent of viral envelope glycoproteins (VEG) and a MAM domain grafted into the latter [6]. [1]. 11429458. Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation. Grandvalet C, Gominet M, Lereclus D;. Microbiology 2001;147:1805-1813. [2]. 10475957. Characterization of the exosporium of Bacillus cereus. Charlton S, Moir AJ, Baillie L, Moir A;. J Appl Microbiol 1999;87:241-245. [3]. 2089225. Molecular characterization of immune inhibitor A, a secreted virulence protease from Bacillus thuringiensis. Lovgren A, Zhang M, Engstrom A, Dalhammar G, Landen R;. Mol Microbiol 1990;4:2137-2146. [4]. 9371455. Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a protease gene downstream of the hly region. Ogierman MA, Fallarino A, Riess T, Williams SG, Attridge SR, Manning PA;. J Bacteriol 1997;179:7072-7080. [5]. 12029046. The InhA2 metalloprotease of Bacillus thuringiensis strain 407 is required for pathogenicity in insects infected via the oral route. Fedhila S, Nel P, Lereclus D;. J Bacteriol 2002;184:3296-3304. [6]. 26745529. Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Se. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold [1]. [1]. 7736581. Polycystic kidney disease: the complete structure of the PKD1 gene and its protein. The International Polycystic Kidney Disease Consortium;. Cell. 1995;81:289-298. [2]. 9889186. The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease. Bycroft M, Bateman A, Clarke J, Hamill SJ, Sandford R, Thomas RL, Chothia C;. EMBO J 1999;18:297-305. (from Pfam)

Date:

2024-10-16

This model describes a metalloproteinase domain, with a characteristic HExxH motif. Examples of this domain are found in proteins in the family of immune inhibitor A, which cleaves antibacterial peptides, and in other, only distantly related proteases. This model is built to be broader and more inclusive than Pfam model PF05547.

Date:

2024-05-30