Protein Family Models

The species-specific Lon-insertion domain (LID) is characteristic of Lon proteases (also known as endopeptidase La) and is fused to the AAA+ module [1]. Bacterial and eukaryotic Lons (LonA) have a LID at the N-terminal of AAA+ module; in archaeal Lons (LonB) the LID, represented in this entry, is inserted within the AAA+ module in a series of transmembrane segments known as the membrane-anchoring region (MA). In the Lon-like protease LonC, which does not have ATPase activity, the LID is also within the AAA-like module similar to LonBs; in this case, it is predicted to contain coiled-coil regions rather than transmembrane segments [1]. [1]. 23897463. Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors. Liao JH, Ihara K, Kuo CI, Huang KF, Wakatsuki S, Wu SH, Chang CI;. Acta Crystallogr D Biol Crystallogr. 2013;69:1395-1402. (from Pfam)

Date:

2025-01-31

This domain represents the helical domain found in the Lon-like LonC protease from Meiothermus taiwanensis [1], a Lon-like protease with no ATPase activity. [1]. 23897463. Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors. Liao JH, Ihara K, Kuo CI, Huang KF, Wakatsuki S, Wu SH, Chang CI;. Acta Crystallogr D Biol Crystallogr. 2013;69:1395-1402. (from Pfam)

Date:

2025-01-31

This entry includes a wide variety of AAA domains, including some that have lost essential nucleotide binding residues in the P-loop. This domain is found in Lon proteases from archaea and bacteria [1]. [1]. 23897463. Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors. Liao JH, Ihara K, Kuo CI, Huang KF, Wakatsuki S, Wu SH, Chang CI;. Acta Crystallogr D Biol Crystallogr. 2013;69:1395-1402. (from Pfam)

Date:

2025-01-31

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:

2025-02-02

Lon protease (S16) family protein is similar to Escherichia coli Lon protease homolog, which may be an ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins, as well as certain short-lived regulatory proteins

Date:

2025-01-11