Protein Domain : IPR000667

Type:  Family Name:  Peptidase S13, D-Ala-D-Ala carboxypeptidase C
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 of serine peptidases belong to MEROPS peptidase family S13 (D-Ala-D-Ala carboxypeptidase C, clan SE). The predicted active site residues for members of this family and family S12 occur in the motif SXXK.D-Ala-D-Ala carboxypeptidase C is involved in the metabolism of cell components []; it is synthesised with a leader peptide to target it to the cell membrane []. After cleavage of the leader peptide, the enzyme is retained in the membrane by a C-terminal anchor []. There are three families of serine-type D-Ala-D-Ala peptidase (designated S11, S12 and S13), which are also known as low molecular weight penicillin-binding proteins [].Family S13 comprises D-Ala-D-Ala peptidases that have sufficient sequence similarity around their active sites to assume a distant evolutionaryrelationship to other clan members; members of the S13 family also bind penicillin and have D-amino-peptidase activity. Proteases of family S11 haveexclusive D-Ala-D-Ala peptidase activity, while some members of S12 are C beta-lactamases []. Short Name:  Peptidase_S13
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0 Child Features

1 Contains

DB identifier Type Name
IPR012338 Domain Beta-lactamase/transpeptidase-like

3 Cross Referencess

Identifier
PF02113
PR00922
TIGR00666

0 Found In

2 GO Annotations

GO Term Gene Name
GO:0004185 IPR000667
GO:0006508 IPR000667

2 Ontology Annotations

GO Term Gene Name
GO:0004185 IPR000667
GO:0006508 IPR000667

0 Parent Features

6 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
35543.m000026 B9TF38 PAC:16826662 Ricinus communis 276  
Pp3s42_370V3.1.p PAC:32945160 Physcomitrium patens 1310  
Brdisv1pangenome1007686m.p PAC:33635476 Brachypodium distachyon Pangenome 428  
Brdisv1pangenome1010521m.p PAC:33623518 Brachypodium distachyon Pangenome 379  
Brdisv1BdTR11A1048531m.p PAC:35688032 Brachypodium distachyon BdTR11a 379  
Brdisv1BdTR11A1042704m.p PAC:35691632 Brachypodium distachyon BdTR11a 428  

3 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8439290
            7845208
            1741619