Protein Family Models

This domain is found at the N-terminal end of ESX-1 secretion system protein EccA1 from Mycobacterium tuberculosis and similar proteins predominantly from Actinobacteria. EccA1 is part of the ESX-1 specialised secretion system (a cluster of the type VII secretion system, T7SS). EccA1 contains a C-terminal ATPase domain (Pfam:PF00004 and Pfam:PF17866) and a tetratricopeptide repeat (TPR) containing N-terminal domain (this entry). The six tandem TPR motifs of this domain packed in parallel create a series of repeating antiparallel alpha-helices that give rise to an overall superhelix structure [1,2]. Paper describing PDB structure 3as4. [1]. 21784982. Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly. Zeytuni N, Ozyamak E, Ben-Harush K, Davidov G, Levin M, Gat Y, Moyal T, Brik A, Komeili A, Zarivach R;. Proc Natl Acad Sci U S A. 2011;108:E480-E487. Paper describing PDB structure 4f3v. [2]. 23818233. Crystal structure of the N-terminal domain of EccA(1) ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis. Wagner JM, Evans TJ, Korotkov KV;. Proteins. 2014;82:159-163. (from Pfam)

Date:

2024-10-16

This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. (from Pfam)

Date:

2024-08-14

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

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

This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc.

Gene:

eccA

Date:

2021-04-27