Protein Family Models

This entry represents the AAA+ ATPase lid domain of Lon proteases [1-5]. Paper describing PDB structure 1qzm. [1]. 15037242. Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution. Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A;. J Struct Biol. 2004;146:113-122. Paper describing PDB structure 3m6a. [2]. 20600124. Crystal structures of Bacillus subtilis Lon protease. Duman RE, Lowe J;. J Mol Biol. 2010;401:653-670. Paper describing PDB structure 4git. [3]. 24531457. Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease. Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH;. Acta Crystallogr D Biol Crystallogr. 2014;70:218-230. Paper describing PDB structure 4ypl. [4]. 27041592. Structural Insights into the Allosteric Operation of the Lon AAA+ Protease. Lin CC, Su SC, Su MY, Liang PH, Feng CC, Wu SH, Chang CI;. Structure. 2016;24:667-675. Paper describing PDB structure 4ypm. [5]. 27041593. Structural Basis for the Magnesium-Dependent Activation and Hexamerization of the Lon AAA+ Protease. Su SC, Lin CC, Tai HC, Chang MY, Ho MR, Babu CS, Liao JH, Wu SH, Chang YC, Lim C, Chang CI;. Structure. 2016;24:676-686. (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

The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops. [1]. 12208506. Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis. Vasilyeva OV, Kolygo KB, Leonova YF, Potapenko NA, Ovchinnikova TV;. FEBS Lett 2002;526:66-70. (from Pfam)

Date:

2024-10-16

This domain has been shown to be part of the PUA superfamily [2]. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, Pfam:PF05362. ATP-dependent Lon proteases are conserved in all living organisms and catalyse rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins. [1]. 16199667. Crystal structure of the N-terminal domain of E. coli Lon protease. Li M, Rasulova F, Melnikov EE, Rotanova TV, Gustchina A, Maurizi MR, Wlodawer A;. Protein Sci. 2005;14:2895-2900. [2]. 19191354. Structural genomics reveals EVE as a new ASCH/PUA-related domain. Bertonati C, Punta M, Fischer M, Yachdav G, Forouhar F, Zhou W, Kuzin AP, Seetharaman J, Abashidze M, Ramelot TA, Kennedy MA, Cort JR, Belachew A, Hunt JF, Tong L, Montelione GT, Rost B;. Proteins. 2009;75:760-773. [3]. 20834233. Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. Cha SS, An YJ, Lee CR, Lee HS, Kim YG, Kim SJ, Kwon KK, De Donatis GM, Lee JH, Maurizi MR, Kang SG;. EMBO J. 2010;29:3520-3530. (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

endopeptidase La is an ATP-dependent serine protease that degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long; it binds to DNA in a double-stranded, site-specific manner

Date:

2023-02-27

Gene:

lon

Date:

2021-07-28

This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock.

Gene:

lon

Date:

2021-07-22