Annotations: 3J83

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF08042	e3j83A1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
A	PPE	e3j83A2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
B	EUF08042	e3j83B2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
B	PPE	e3j83B1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
C	EUF08042	e3j83C2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
C	PPE	e3j83C1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
D	EUF08042	e3j83D1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
D	PPE	e3j83D2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
E	EUF08042	e3j83E1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
E	PPE	e3j83E2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
F	EUF08042	e3j83F2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
F	PPE	e3j83F1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
G	EUF08042	e3j83G2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: EUF08042	ECOD (1.6)
G	PPE	e3j83G1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	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	PF21856	ESX-1 secretion-associated protein EspB, PPE domain (EspB_PPE)	ESX-1 secretion-associated protein EspB, PPE domain	This entry represents the PPe domain of ESX-1 secretion- associated protein EspB, a member of the PE/PPE family and the only one described to date to form higher-order oligomers [1-3]. It contains PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-t ...	This entry represents the PPe domain of ESX-1 secretion- associated protein EspB, a member of the PE/PPE family and the only one described to date to form higher-order oligomers [1-3]. It contains PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. EspB oligomerises into a cylinder-like heptamer through its N-terminal domain, that form channel-like structures [1-3].	Domain
A, B, C, D, E A, B, C, D, E, F, G	PF18625	ESX-1 secreted protein B PE domain (EspB_PE)	ESX-1 secreted protein B PE domain	The ESX-1 secretion system is an important virulence determinant in Mycobacterium tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protea ...	The ESX-1 secretion system is an important virulence determinant in Mycobacterium tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. This domain represents the PE domain located at the N-terminal region of EspB which carries the conserved YxxxD/E secretion motif [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	ESX-1 secretion-associated protein EspB	identical protein binding protein binding binding	biological process involved in interspecies interaction between organisms biological process involved in interaction with host biological process involved in symbiotic interaction protein localization establishment of protein localization cellular localization nitrogen compound transport transport secretion establishment of protein localization to extracellular region export from cell protein secretion establishment of localization protein secretion by the type VII secretion system biological process involved in interspecies interaction between organisms biological process involved in interaction with host biological process involved in symbiotic interaction protein localization establishment of protein localization cellular localization nitrogen compound transport transport secretion establishment of protein localization to extracellular region export from cell protein secretion establishment of localization protein secretion by the type VII secretion system protein localization to extracellular region transmembrane transport localization secretion by cell protein transmembrane transport protein transport cellular macromolecule localization macromolecule localization cellular process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G	IPR041275	ESX-1 secretion-associated protein EspB, PE domain	Domain
A, B, C, D, E A, B, C, D, E, F, G	IPR054056	ESX-1 secretion-associated protein EspB, PPE domain	Domain
A, B, C, D, E A, B, C, D, E, F, G	IPR038332	PPE superfamily	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 R01GM157729.