Annotations: 3EMF

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF15403,PF18669	e3emfA1	A: beta duplicates or obligate multimers	X: Trimeric autotransporter adhesin Trp ring domain (From Topology)	H: Trimeric autotransporter adhesin Trp ring domain (From Topology)	T: Trimeric autotransporter adhesin Trp ring domain	F: PF15403,PF18669	ECOD (1.6)
B	PF15403,PF18669	e3emfB1	A: beta duplicates or obligate multimers	X: Trimeric autotransporter adhesin Trp ring domain (From Topology)	H: Trimeric autotransporter adhesin Trp ring domain (From Topology)	T: Trimeric autotransporter adhesin Trp ring domain	F: PF15403,PF18669	ECOD (1.6)
C	PF15403,PF18669	e3emfC1	A: beta duplicates or obligate multimers	X: Trimeric autotransporter adhesin Trp ring domain (From Topology)	H: Trimeric autotransporter adhesin Trp ring domain (From Topology)	T: Trimeric autotransporter adhesin Trp ring domain	F: PF15403,PF18669	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1780.10	Alpha Beta	Alpha-Beta Complex	Trimeric adhesin	Trimeric adhesin	CATH (4.3.0)
B	3.90.1780.10	Alpha Beta	Alpha-Beta Complex	Trimeric adhesin	Trimeric adhesin	CATH (4.3.0)
C	3.90.1780.10	Alpha Beta	Alpha-Beta Complex	Trimeric adhesin	Trimeric adhesin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF15403	HiaBD2_N domain of Trimeric autotransporter adhesin (GIN) (HiaBD2)	HiaBD2_N domain of Trimeric autotransporter adhesin (GIN)	-	Motif
A, B, C	PF18669	Trimeric autotransporter adhesin Trp ring domain (Trp_ring)	Trimeric autotransporter adhesin Trp ring domain	Autotransporters are synthesized as precursor proteins with three functional domains, namely, an N-terminal signal peptide, an internal passenger domain, and a C-terminal pore-forming translocator domain. The C-terminal translocator domain is embedd ...	Autotransporters are synthesized as precursor proteins with three functional domains, namely, an N-terminal signal peptide, an internal passenger domain, and a C-terminal pore-forming translocator domain. The C-terminal translocator domain is embedded in the outer membrane and facilitates delivery of the internal passenger domain to the bacterial surface. In conventional autotransporters, the C-terminal translocator domain contains approximately 300 amino acids and is monomeric. In contrast, in trimeric autotransporters, the translocator domain contains 60 to 70 amino acids and forms trimers in the outer membrane [1]. This entry represents a Trp-ring domain which is found in the translocator region of H. influenzae Hia autotransporter, an adhesive protein that promotes adherence to respiratory epithelial cells [2]. Trp-ring domains appear to be crucial repeated modular units in Hia, both in the general architecture of the passenger domain and in the structure of the binding domains [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Hia (Adhesin)	-	-	cell surface cellular anatomical entity membrane outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR040482	Trimeric autotransporter adhesin, Trp ring domain	Domain
A, B, C	IPR008635	Trimeric autotransporter adhesin YadA-like, stalk domain	Domain
A, B, C	IPR028230	Trimeric autotransporter adhesin, tryptophan-ring motif	Domain
A, B, C	IPR037174	Trimeric adhesin	Homologous Superfamily
A, B, C	IPR005594	Trimeric autotransporter adhesin YadA-like, C-terminal membrane anchor domain	Domain
A, B, C	IPR024973	ESPR domain	Domain
A, B, C	IPR029275	Trimeric autotransporter adhesin, putative GIN domain	Domain
A, B, C	IPR045584	Pilin-like	Homologous Superfamily

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 R01GM133198.