4KXR

Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG5 in complex with PE25-PPE41 dimer

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4kxra_	All alpha proteins	Ferritin-like	PE/PPE dimer-like	PE	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
B	d4kxrb_	All alpha proteins	Ferritin-like	PE/PPE dimer-like	PPE	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	PE/PPE dimer-like	8041619	3001123	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	PE	e4kxrA1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PE (From Topology)	T: PE	F: PE	ECOD (1.6)
B	PPE	e4kxrB1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: PPE (From Topology)	T: PPE	F: PPE	ECOD (1.6)
C	ESX-1_EspG	e4kxrC1	A: a+b two layers	X: MybT EspG5 chaperone (From Topology)	H: MybT EspG5 chaperone (From Topology)	T: MybT EspG5 chaperone	F: ESX-1_EspG	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	CATH (4.3.0)
B	1.20.1260.20	Mainly Alpha	Up-down Bundle	Ferritin	PPE superfamily	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00934	PE family (PE)	PE family	-	Family
B	PF00823	PPE family (PPE)	PPE family	-	Family
C	PF14011	EspG family (ESX-1_EspG)	EspG family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PE25	protein heterodimerization activity protein binding binding protein dimerization activity	protein-containing complex organization protein trimerization protein heterotrimerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein-containing complex assembly cellular process cellular component organization or biogenesis protein heterooligomerization	extracellular region cellular anatomical entity
B	PPE41	-	response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to defenses of other organism response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction response to host immune response response to host response to external biotic stimulus	cell surface cellular anatomical entity extracellular region
C	EspG5	-	-	cell periphery plasma membrane membrane cellular anatomical entity external encapsulating structure cell wall peptidoglycan-based cell wall intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000084	PE-PGRS family, N-terminal	Domain
B	IPR038332	PPE superfamily	Homologous Superfamily
B	IPR000030	PPE domain	Domain
C	IPR025734	EspG family	Family

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.