5WTL

Crystal structure of the periplasmic portion of outer membrane protein A (OmpA) from Capnocytophaga gingivalis

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	OmpA-like	8075224	3001650	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	OmpA-like	8075224	3001650	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	OmpA-like	8075224	3001650	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	OmpA-like	8075224	3001650	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)
A	PF00691	e5wtlA2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: OmpA-like (From Topology)	T: OmpA-like	F: PF00691	ECOD (1.6)
A	PF02412	e5wtlA1	A: few secondary structure elements	X: TSP type-3 repeat (From Topology)	H: TSP type-3 repeat (From Topology)	T: TSP type-3 repeat	F: PF02412	ECOD (1.6)
B	PF00691	e5wtlB2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: OmpA-like (From Topology)	T: OmpA-like	F: PF00691	ECOD (1.6)
B	PF02412	e5wtlB1	A: few secondary structure elements	X: TSP type-3 repeat (From Topology)	H: TSP type-3 repeat (From Topology)	T: TSP type-3 repeat	F: PF02412	ECOD (1.6)
C	PF00691	e5wtlC1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: OmpA-like (From Topology)	T: OmpA-like	F: PF00691	ECOD (1.6)
C	PF02412	e5wtlC2	A: few secondary structure elements	X: TSP type-3 repeat (From Topology)	H: TSP type-3 repeat (From Topology)	T: TSP type-3 repeat	F: PF02412	ECOD (1.6)
D	PF00691	e5wtlD1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: OmpA-like (From Topology)	T: OmpA-like	F: PF00691	ECOD (1.6)
D	PF02412	e5wtlD2	A: few secondary structure elements	X: TSP type-3 repeat (From Topology)	H: TSP type-3 repeat (From Topology)	T: TSP type-3 repeat	F: PF02412	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00691	OmpA family (OmpA)	OmpA family	-	Family
A, B, C, D	PF02412	Thrombospondin type 3 repeat (TSP_3)	Thrombospondin type 3 repeat	The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats [1]. The repeat lacks defined secondary structure [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	OmpA family protein	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding wide pore channel activity passive transmembrane transporter activity channel activity porin activity transporter activity transmembrane transporter activity	cell adhesion cellular process localization transport monoatomic ion transport establishment of localization	protein-containing complex membrane pore complex membrane protein complex cellular anatomical entity cell periphery cell outer membrane external encapsulating structure cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR006664	Outer membrane protein, bacterial	Domain
A, B, C, D	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A, B, C, D	IPR003367	Thrombospondin, type 3-like repeat	Repeat
A, B, C, D	IPR028974	TSP type-3 repeat	Homologous Superfamily
A, B, C, D	IPR036737	OmpA-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR011250	Outer membrane protein/outer membrane enzyme PagP, beta-barrel	Homologous Superfamily
A, B, C, D	IPR006665	OmpA-like domain	Domain
A, B, C, D	IPR027385	Outer membrane protein beta-barrel domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.