1O82

X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d1o82c_	All alpha proteins	Saposin-like	Bacteriocin AS-48	Bacteriocin AS-48	Bacteriocin AS-48	(Enterococcus faecalis ) [TaxId: 1351 ],	SCOPe (2.08)
D	d1o82d_	All alpha proteins	Saposin-like	Bacteriocin AS-48	Bacteriocin AS-48	Bacteriocin AS-48	(Enterococcus faecalis ) [TaxId: 1351 ],	SCOPe (2.08)
A	d1o82a_	All alpha proteins	Saposin-like	Bacteriocin AS-48	Bacteriocin AS-48	Bacteriocin AS-48	(Enterococcus faecalis ) [TaxId: 1351 ],	SCOPe (2.08)
B	d1o82b_	All alpha proteins	Saposin-like	Bacteriocin AS-48	Bacteriocin AS-48	Bacteriocin AS-48	(Enterococcus faecalis ) [TaxId: 1351 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	Circular bacteriocins	8037326	3000616	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Circular bacteriocins	8037326	3000616	SCOP2B (2022-06-29)
A	SCOP2 Family	Uberolysin-like	8024947	4001060	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Circular bacteriocins	8037326	3000616	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Circular bacteriocins	8037326	3000616	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	Bacteriocin_IId	e1o82C1	A: alpha arrays	X: Saposin-like	H: Bacteriocin AS-48-related (From Topology)	T: Bacteriocin AS-48-related	F: Bacteriocin_IId	ECOD (1.6)
D	Bacteriocin_IId	e1o82D1	A: alpha arrays	X: Saposin-like	H: Bacteriocin AS-48-related (From Topology)	T: Bacteriocin AS-48-related	F: Bacteriocin_IId	ECOD (1.6)
A	Bacteriocin_IId	e1o82A1	A: alpha arrays	X: Saposin-like	H: Bacteriocin AS-48-related (From Topology)	T: Bacteriocin AS-48-related	F: Bacteriocin_IId	ECOD (1.6)
B	Bacteriocin_IId	e1o82B1	A: alpha arrays	X: Saposin-like	H: Bacteriocin AS-48-related (From Topology)	T: Bacteriocin AS-48-related	F: Bacteriocin_IId	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	1.20.225.10	Mainly Alpha	Up-down Bundle	Bacteriocin As-48	Chain A	CATH (4.3.0)
D	1.20.225.10	Mainly Alpha	Up-down Bundle	Bacteriocin As-48	Chain A	CATH (4.3.0)
A	1.20.225.10	Mainly Alpha	Up-down Bundle	Bacteriocin As-48	Chain A	CATH (4.3.0)
B	1.20.225.10	Mainly Alpha	Up-down Bundle	Bacteriocin As-48	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF09221	Bacteriocin class IId cyclical uberolysin-like (Bacteriocin_IId)	Bacteriocin class IId cyclical uberolysin-like	Members of this family are membrane-interacting peptides, produced by Firmicutes that display a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. They adopt a helical structure, with four or five alpha helices forming a ...	Members of this family are membrane-interacting peptides, produced by Firmicutes that display a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. They adopt a helical structure, with four or five alpha helices forming a Saposin-like fold [2,5]. The structure has been found to be cyclical [1, 3, 5]. It should be pointed out that one reference [4] implies that both circularin A and gassericin A are class V or IIc-type bacteriocins; however we find that these two proteins fall into different Pfam families families, this one and BacteriocIIc_cy, Pfam:PF12173.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	PEPTIDE ANTIBIOTIC AS-48	-	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus cellular process disruption of cell in another organism disruption of anatomical structure in another organism biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus cellular process disruption of cell in another organism disruption of anatomical structure in another organism killing of cells of another organism cell killing	cellular anatomical structure membrane extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR009086	Bacteriocin AS-48	Homologous Superfamily
A, B, C, D	IPR020038	Circular bacteriocin	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D	OPM	Monotopic/peripheral	All alpha monotopic/peripheral	Bacteriocin, class II	Bacteriocin IId

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.