7UKJ

In situ cryo-EM structure of bacteriophage Sf6 portal:gp7 complex at 2.7A resolution

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF21519	e7ukjA3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Ig-like domain in tailspike protein (From Topology)	T: Ig-like domain in tailspike protein	F: PF21519	ECOD (1.6)
A	PF09008	e7ukjA2	A: beta sandwiches	X: Head-binding domain of phage P22 tailspike protein (From Topology)	H: Head-binding domain of phage P22 tailspike protein (From Topology)	T: Head-binding domain of phage P22 tailspike protein	F: PF09008	ECOD (1.6)
A	F_UNCLASSIFIED	e7ukjA1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF21519	e7ukjB3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Ig-like domain in tailspike protein (From Topology)	T: Ig-like domain in tailspike protein	F: PF21519	ECOD (1.6)
B	PF09008	e7ukjB2	A: beta sandwiches	X: Head-binding domain of phage P22 tailspike protein (From Topology)	H: Head-binding domain of phage P22 tailspike protein (From Topology)	T: Head-binding domain of phage P22 tailspike protein	F: PF09008	ECOD (1.6)
B	F_UNCLASSIFIED	e7ukjB1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)
C	PF21519	e7ukjC3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Ig-like domain in tailspike protein (From Topology)	T: Ig-like domain in tailspike protein	F: PF21519	ECOD (1.6)
C	PF09008	e7ukjC2	A: beta sandwiches	X: Head-binding domain of phage P22 tailspike protein (From Topology)	H: Head-binding domain of phage P22 tailspike protein (From Topology)	T: Head-binding domain of phage P22 tailspike protein	F: PF09008	ECOD (1.6)
C	F_UNCLASSIFIED	e7ukjC1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: F_UNCLASSIFIED	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF21519	Tailspike protein, C-terminal (Tailspike_C)	Tailspike protein, C-terminal	Tailspike protein from Shigella phage Sf6 specifically mediates the attachment to their hosts. Its structure revealed a conserved architecture with a central, right-handed beta-helix. The C-terminal domain adopts a beta-sandwich fold, is represented ...	Tailspike protein from Shigella phage Sf6 specifically mediates the attachment to their hosts. Its structure revealed a conserved architecture with a central, right-handed beta-helix. The C-terminal domain adopts a beta-sandwich fold, is represented in this entry, and is reminiscent of viral capsid proteins [1,2].	Domain
A, B, C	PF12708	Pectate lyase superfamily protein (Pectate_lyase_3)	Pectate lyase superfamily protein	-	Repeat
A, B, C	PF09008	Head binding (Head_binding)	Head binding	The head binding domain found in the Phage P22 tailspike protein contains two regular beta-sheets, A and B, oriented nearly perpendicular to each other and composed of five and three strands respectively. The topology of the strands is exclusively an ...	The head binding domain found in the Phage P22 tailspike protein contains two regular beta-sheets, A and B, oriented nearly perpendicular to each other and composed of five and three strands respectively. The topology of the strands is exclusively antiparallel. The tailspike protein trimerises through this domain, and the direction of the strands with respect to the molecular triad is almost parallel for beta-sheet A, whereas beta-sheet B is perpendicular to the triad, forming a dome-like structure. This domain is dispensable for thermostability and SDS resistance of the intact protein, and its deletion has only minor effects on tailspike folding kinetics [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Gene 14 protein	hydrolase activity, acting on glycosyl bonds endo-1,3-alpha-L-rhamnosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	biological process involved in interspecies interaction between organisms symbiont entry into host biological process involved in interaction with host biological process involved in symbiotic interaction virion attachment to host cell adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host symbiont-mediated disruption of host anatomical structure symbiont-mediated disruption of host cell envelope symbiont entry into host cell via disruption of host cell envelope symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell biological process involved in interspecies interaction between organisms symbiont entry into host biological process involved in interaction with host biological process involved in symbiotic interaction virion attachment to host cell adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host symbiont-mediated disruption of host anatomical structure symbiont-mediated disruption of host cell envelope symbiont entry into host cell via disruption of host cell envelope symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell disruption of anatomical structure in another organism metabolic process symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide disruption of cell wall in another organism symbiont-mediated disruption of host cell wall disruption of cellular anatomical structure in another organism	virus tail, fiber virus tail virion component

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR012334	Pectin lyase fold	Homologous Superfamily
A, B, C	IPR036730	Phage P22 tailspike-like, N-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR049104	Tail spike protein-like, C-terminal domain	Domain
A, B, C	IPR024535	Pectate lyase superfamily protein	Domain
A, B, C	IPR009093	Bacteriophage P22 tailspike, N-terminal	Domain
A, B, C	IPR011050	Pectin lyase fold/virulence factor	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.