Protein Domain : IPR011782

Type:  Family Name:  Peptidase S1C, Do
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 family consists serine peptidases belonging to MEROPS peptidase family S1, subfamily S1C (protease Do, clan PA(S)). They are variously designated DegP, DegQ, heat shock protein HtrA, MucD and protease DO. The ortholog in Pseudomonas aeruginosais designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in Escherichia coliwhich can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens []. The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures []. Short Name:  Pept_S1C_Do
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0 Child Features

2 Contains

DB identifier Type Name
IPR001478 Domain PDZ domain
IPR001254 Domain Serine proteases, trypsin domain

1 Cross References

Identifier
TIGR02037

0 Found In

2 GO Annotations

GO Term Gene Name
GO:0004252 IPR011782
GO:0006508 IPR011782

2 Ontology Annotations

GO Term Gene Name
GO:0004252 IPR011782
GO:0006508 IPR011782

1 Parent Features

DB identifier Type Name
IPR001940 Family Peptidase S1C

5 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Araha.11756s0430.1.p PAC:28856649 Arabidopsis halleri 478  
Brdisv1pangenome1008666m.p PAC:33619995 Brachypodium distachyon Pangenome 387  
Brdisv1BdTR11A1040359m.p PAC:35691479 Brachypodium distachyon BdTR11a 605  
Brdisv1BdTR11A1040393m.p PAC:35695119 Brachypodium distachyon BdTR11a 387  
Brdisv1BdTR11A1040382m.p PAC:35695718 Brachypodium distachyon BdTR11a 454  

4 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8439290
            7845208
            11919638
            12458220