Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyPeptidoglycan binding domain PGBD8024382 4000784 SCOP2 (2022-06-29)
ASCOP2 FamilyMuramoyl-pentapeptide carboxypeptidase8023353 4001391 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyPGBD-like8036761 3001357 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyHedgehog/DD-peptidase8035733 3001458 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APG_binding_1e1lbuA1 A: alpha arraysX: PGBD-like (From Topology)H: PGBD-like (From Topology)T: PGBD-likeF: PG_binding_1ECOD (1.6)
APeptidase_M15_3e1lbuA2 A: a+b two layersX: Hedgehog/DD-peptidase (From Topology)H: Hedgehog/DD-peptidase (From Topology)T: Hedgehog/DD-peptidaseF: Peptidase_M15_3ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.10.101.10 Mainly Alpha Orthogonal Bundle Muramoyl-pentapeptide Carboxypeptidase domain 1CATH (4.3.0)
A3.30.1380.10 Alpha Beta 2-Layer Sandwich Muramoyl-pentapeptide Carboxypeptidase domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01471Putative peptidoglycan binding domain (PG_binding_1)Putative peptidoglycan binding domainThis domain is composed of three alpha helices [1]. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation [2]. This domain may have a general peptidoglycan binding function. This family is ...This domain is composed of three alpha helices [1]. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation [2]. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins [3]. The domain is found to bind peptidoglycan experimentally [4].
Domain
PF08291Peptidase M15 (Peptidase_M15_3)Peptidase M15- Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
zinc D-Ala-D-Ala carboxypeptidase  M-CSA #585

The zinc D-Ala-D-Ala carboxypeptidase belongs to the peptidase M15 family and hydrolyses the C-terminal peptide bond of the peptides of general structure R-DAla-D-Xaa, it is secreted by Streptomyces albus G. The lytic activity of the enzyme and its extracellular location suggest that it might be used by Streptomyces for fighting competitors in its ecological niche, since the enzyme does not hydrolyse the Streptomyces peptidoglycan.

Defined by 7 residues: HIS:A-154ASP:A-161TYR:A-189HIS:A-192ASP:A-194HIS:A-195HIS:A-197
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