Protein Family Models

This Pfam entry includes some of the AAA proteins not detected by the Pfam:PF00004 model. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Date:

2024-08-14

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

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)

Date:

2024-10-16

Magnesium-chelatase is a three-component enzyme that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa. [1]. 9359397. Mechanism and regulation of Mg-chelatase. Walker CJ, Willows RD;. Biochem J 1997;327:321-333. [2]. 9457877. Reconstitution of an active magnesium chelatase enzyme complex from the bchI, -D, and -H gene products of the green sulfur bacterium Chlorobium vibrioforme expressed in Escherichia coli. Petersen BL, Jensen PE, Gibson LC, Stummann BM, Hunter CN, Henningsen KW;. J Bacteriol 1998;180:699-704. (from Pfam)

Date:

2024-10-16

sigma-54-dependent transcriptional regulator containing sigma-54 interaction, PRD, and PTS_IIA_man-related domains

Date:

2019-03-21