InterPro : IPR015956

Name  Penicillin-binding protein-associated Short Name  Peniciliin-bd_prot-assoc
Type  Domain Description  This entry represents a structural motif found at the C-terminal of penicillin-binding proteins 4 (PBP4) and 5 (PBP5), as well as at the C-terminal of D-Ala-D-Ala carboxypeptidase A, a member of the MEROPS S11 peptidase family (PBP4 and PBP5 also belong to this peptidase family). These domains share a similar structure, consisting of a beta-sandwich of six strands in two sheets [, ].Penicillin-binding proteins are beta-lactam antibiotic-sensitive bacterial enzymes required for the growth and maintenance of the peptidoglycan layer of the bacterial cell wall that protects the cell from osmotic stress. PBP4 functions as a transpeptidase, acting co-operatively with PBP2 in staphylococcal cell wall biosynthesis and susceptibility to antimicrobial agents [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR012907 Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal Peptidase_S11_C Domain
IPR015294 Penicillin-binding protein 4, C-terminal domain Pen-bd_prot4_C_dom Domain

0 Contains

1 Found In

Id Name Short Name Type
IPR018044 Peptidase S11, D-alanyl-D-alanine carboxypeptidase A Peptidase_S11 Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Nicholas RA Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex. 2003 J Biol Chem 278 52826-33
Morlot C Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae. 2005 J Biol Chem 280 15984-91
Kishida H Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. 2006 Biochemistry 45 783-92

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)