4UW8 | pdb_00004uw8

Structure of the carboxy-terminal domain of the bacteriophage T5 L- shaped tail fiber with its intra-molecular chaperone domain

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)
B	EUF07874	e4uw8B2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
B	Peptidase_S74	e4uw8B1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
A	EUF07874	e4uw8A2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
A	Peptidase_S74	e4uw8A1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
C	EUF07874	e4uw8C2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
C	Peptidase_S74	e4uw8C1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
D	EUF07874	e4uw8D2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
D	Peptidase_S74	e4uw8D1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
E	EUF07874	e4uw8E2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
E	Peptidase_S74	e4uw8E1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
F	EUF07874	e4uw8F2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
F	Peptidase_S74	e4uw8F1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
G	EUF07874	e4uw8G2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
G	Peptidase_S74	e4uw8G1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
H	EUF07874	e4uw8H1	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
H	Peptidase_S74	e4uw8H2	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)
I	EUF07874	e4uw8I2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: EUF07874	ECOD (1.6)
I	Peptidase_S74	e4uw8I1	A: alpha arrays	X: Intramolecular chaperone domain in virus tail spike protein (From Topology)	H: Intramolecular chaperone domain in virus tail spike protein (From Topology)	T: Intramolecular chaperone domain in virus tail spike protein	F: Peptidase_S74	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I	PF13884	Chaperone of endosialidase (Peptidase_S74)	Chaperone of endosialidase	This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the fi ...	This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, Pfam:PF12219. The endosialidase protein forms homotrimeric molecules in bacteriophages [1]. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I	L-SHAPED TAIL FIBER PROTEIN	peptidase activity serine hydrolase activity catalytic activity, acting on a protein serine-type peptidase activity hydrolase activity catalytic activity	virion attachment to host cell biological process involved in interspecies interaction between organisms receptor-mediated virion attachment to host cell adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host adhesion receptor-mediated virion attachment to host cell biological process involved in interaction with host biological process involved in symbiotic interaction proteolysis metabolic process cellular process primary metabolic process virion attachment to host cell biological process involved in interspecies interaction between organisms receptor-mediated virion attachment to host cell adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host adhesion receptor-mediated virion attachment to host cell biological process involved in interaction with host biological process involved in symbiotic interaction proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process symbiont entry into host cell symbiont entry into host lipopolysaccharide-mediated virion attachment to host cell	virus tail, fiber virus tail virion component

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR030392	Intramolecular chaperone auto-processing domain	Domain

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.