InterPro : IPR008268

Name  Peptidase S16, active site Short Name  Peptidase_S16_AS
Type  Active_site Description  Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].This signature defines the active site of the serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SF). These proteases which are dependent on the hydrolysis of ATP for their activity and have a serine in their active site, they include:Bacterial ATP-dependent proteases [, ]. The prototype of those bacterial enzymes is the Escherichia coliLa protease () (gene lon). La is capable of hydrolysing large proteins; it degrades short-lived regulatory (such as rcsA and sulA) and abnormal proteins. It is a cytoplasmic protein of 87 kDa that associates as an homotetramer. Its proteolytic activity is stimulated by single-stranded DNA.Eukaryotic mitochondrial matrix proteases [, ]. The prototype of these enzymes is the yeast PIM1 protease. It is a mitochondrial matrix protein of 120 kDa that associated as an homohexamer. It catalyses the initial step of mitochondrial protein degradation.Haemophilus influenzaelon-B (HI1324), a protein which does not contain the ATP-binding domain, but possess a slightly divergent form of the catalytic domain.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

6 Found In

Id Name Short Name Type
IPR020568 Ribosomal protein S5 domain 2-type fold Ribosomal_S5_D2-typ_fold Domain
IPR008269 Peptidase S16, Lon C-terminal Pept_S16_C Domain
IPR004815 Lon protease, bacterial/eukaryotic-type Lon_bac/euk-typ Family
IPR004663 Lon protease, archaeal Lon_arc Family
IPR014251 Sporulation protease LonB Spore_LonB Family
IPR014252 Sporulation protease LonC Spore_LonC Family

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Rawlings ND Evolutionary families of peptidases. 1993 Biochem J 290 ( Pt 1) 205-18
Rawlings ND Families of serine peptidases. 1994 Methods Enzymol 244 19-61
Van Dyck L PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. 1994 J Biol Chem 269 238-42
Wang N A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. 1993 Proc Natl Acad Sci U S A 90 11247-51
Thomas CD Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease. 1993 Gene 136 237-42
Tojo N The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthus. 1993 J Bacteriol 175 4545-9

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)