Protein Family Models

This family of serine peptidases belong to MEROPS peptidase family S13 (D-Ala-D-Ala carboxypeptidase C, clan SE). The active site residues occur in the motif SXXK. D-Ala-D-Ala carboxypeptidase C is involved in the metabolism of cell components [1,2]. 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 evolutionary relationship to other clan members; members of the S13 family also bind penicillin and have D-amino-peptidase activity [3,4]. [1]. 16411754. Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR;. Biochemistry. 2006;45:783-792. [2]. 1741619. Serine beta-lactamases and penicillin-binding proteins. Ghuysen JM;. Annu Rev Microbiol. 1991;45:37-67. [3]. 7845208. Families of Serine Peptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1994;244:19-61. (from Pfam)

Date:

2024-10-16

D-alanyl-D-alanine carboxypeptidase catalyzes the peptide bond cleavage of D-alanyl-D-alanine to form D-alanine

Date:

2015-10-27

Gene:

dacB

Date:

2021-08-26

In E. coli, this protein is known as penicillin binding protein 4 (dacB). A signal sequence is cleaved from a precursor form. The protein is described as periplasmic in E. coli (Gram-negative) and extracellular in Actinomadura R39 (Gram-positive). Unlike some other proteins with similar activity, it does not form transpeptidation. It is not essential for viability. This family is related to class A beta-lactamases.

Gene:

dacB

Date:

2021-05-12