Protein Family Models

Core MoxR component domain of the MoxR-vWA-beta-propeller ternary systems, a class of NTP-dependent biological conflict systems. [1]. 32101166. Highly regulated, diversifying NTP-dependent biological conflict systems with implications for the emergence of multicellularity. Kaur G, Burroughs AM, Iyer LM, Aravind L;. Elife. 2020; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

This is the LARA (LdcI Associating domain of RavA) domain of bacterial regulatory ATPase RavA (Regulatory ATPase variant A) [1,2]. It adopts an unique fold which consists of a compact antiparallel beta-barrel- like structure formed by six beta-strands and one alpha-helix [1,2]. This domain mediates the interaction between RavA and LdcI (inducible lysine decarboxylase) which form a cage-like complex proposed to assist assembly of specific respiratory complexes in E. coli [2]. [1]. 21148420. Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. El Bakkouri M, Gutsche I, Kanjee U, Zhao B, Yu M, Goret G, Schoehn G, Burmeister WP, Houry WA;. Proc Natl Acad Sci U S A. 2010;107:22499-22504. [2]. 31992852. Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex. Jessop M, Arragain B, Miras R, Fraudeau A, Huard K, Bacia-Verloop M, Catty P, Felix J, Malet H, Gutsche I;. Commun Biol. 2020;3:46. (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. [1]. 21148420. Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. El Bakkouri M, Gutsche I, Kanjee U, Zhao B, Yu M, Goret G, Schoehn G, Burmeister WP, Houry WA;. Proc Natl Acad Sci U S A. 2010;107:22499-22504. [2]. 25097238. Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. Malet H, Liu K, El Bakkouri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I;. Elife. 2014;3:e03653. (from Pfam)

Date:

2024-10-16

This domain is found at the C-terminal of bacterial regulatory ATPase RavA (Regulatory ATPase variant A) [1,2] and is the second subdomain that forms the discontinuous triple helical domain [1]. RavA forms an hexamer in which the triple helical domain mediates the lateral interactions between neighbouring RavA monomers [2]. [1]. 21148420. Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. El Bakkouri M, Gutsche I, Kanjee U, Zhao B, Yu M, Goret G, Schoehn G, Burmeister WP, Houry WA;. Proc Natl Acad Sci U S A. 2010;107:22499-22504. [2]. 31992852. Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex. Jessop M, Arragain B, Miras R, Fraudeau A, Huard K, Bacia-Verloop M, Catty P, Felix J, Malet H, Gutsche I;. Commun Biol. 2020;3:46. (from Pfam)

Date:

2024-10-16

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

ATPase RavA may play a role in metal insertion (metal-chelatase) or as a chaperone

Date:

2019-07-23

Interacts with LdcI, lysine decarboxylase; may be active in late log/ early stationary phase

Gene:

ravA

Date:

2021-09-22