Protein Family Models

M regulator protein trans-acting positive regulator (Mga) is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions [1]. This domain is found in the centre of the Mga proteins. This family also contains a number of bacterial RofA transcriptional regulators that seem to be largely restricted to streptococci. These proteins have been shown to regulate the expression of important bacterial adhesins [2]. This is presumably a DNA-binding domain. [1]. 11952907. Two DNA-binding domains of Mga are required for virulence gene activation in the group A streptococcus. McIver KS, Myles RL;. Mol Microbiol 2002;43:1591-1601. [2]. 11988525. Group A streptococcal RofA-type global regulators exhibit a strain-specific genomic presence and regulation pattern. Kreikemeyer B, Beckert S, Braun-Kiewnick A, Podbielski A;. Microbiology 2002;148:1501-1511. (from Pfam)

Date:

2024-10-16

The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterised by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators Pfam:PF03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99, [2]) and inactive state (pdb:1tlv [4]), revealing massive structural rearrangements upon activation. [1]. 11751049. Structural insights into the regulation of bacterial signalling proteins containing PRDs. van Tilbeurgh H, Declerck N;. Curr Opin Struct Biol 2001;11:685-693. [2]. 11447120. Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator. van Tilbeurgh H, Le Coq D, Declerck N;. EMBO J 2001;20:3789-3799. [3]. 11733988. Dimer stabilization upon activation of the transcriptional antiterminator LicT. Declerck N, Dutartre H, Receveur V, Dubois V, Royer C, Aymerich S, van Tilbeurgh H;. J Mol Biol 2001;314:671-681. [4]. 15699035. Activation of the LicT tran. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

BglG family transcription antiterminator similar to Bacillus subtilis transcriptional regulator MtlR that positively regulates the expression of the mtlAFD operon, which is involved in the uptake and catabolism of mannitol

Date:

2024-07-17