1YJ7 | pdb_00001yj7

Crystal structure of enteropathogenic E.coli (EPEC) type III secretion system protein EscJ

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	YscJ/PrgK C-terminal domain-like	8049144	4006370	SCOP2 (2022-06-29)
A	SCOP2 Family	YscJ/PrgK N-terminal domain-like	8092188	4007764	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	BON domain-like	8092189	3002566	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	NRho-like	8092190	3002569	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	BON domain-like	8092189	3002566	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	NRho-like	8092190	3002569	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	BON domain-like	8092189	3002566	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	NRho-like	8092190	3002569	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	NRho-like	8092190	3002569	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	BON domain-like	8092189	3002566	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	YscJ_FliF	e1yj7A1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif I in type III secretion system (From Topology)	T: Ring-building motif I in type III secretion system	F: YscJ_FliF	ECOD (1.6)
A	PRK15324	e1yj7A2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif II in type III secretion system (From Topology)	T: Ring-building motif II in type III secretion system	F: PRK15324	ECOD (1.6)
B	YscJ_FliF	e1yj7B1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif I in type III secretion system (From Topology)	T: Ring-building motif I in type III secretion system	F: YscJ_FliF	ECOD (1.6)
B	PRK15324	e1yj7B2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif II in type III secretion system (From Topology)	T: Ring-building motif II in type III secretion system	F: PRK15324	ECOD (1.6)
C	YscJ_FliF	e1yj7C1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif I in type III secretion system (From Topology)	T: Ring-building motif I in type III secretion system	F: YscJ_FliF	ECOD (1.6)
C	PRK15324	e1yj7C2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif II in type III secretion system (From Topology)	T: Ring-building motif II in type III secretion system	F: PRK15324	ECOD (1.6)
D	YscJ_FliF	e1yj7D1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif I in type III secretion system (From Topology)	T: Ring-building motif I in type III secretion system	F: YscJ_FliF	ECOD (1.6)
D	PRK15324	e1yj7D2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: Ring-building motif II in type III secretion system (From Topology)	T: Ring-building motif II in type III secretion system	F: PRK15324	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.1530	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Hypothetical protein rpa1041	CATH (4.3.0)
A	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
B	3.30.70.1530	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Hypothetical protein rpa1041	CATH (4.3.0)
B	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
C	3.30.70.1530	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Hypothetical protein rpa1041	CATH (4.3.0)
C	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
D	3.30.70.1530	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Hypothetical protein rpa1041	CATH (4.3.0)
D	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01514	Secretory protein of YscJ/FliF family (YscJ_FliF)	Secretory protein of YscJ/FliF family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	escJ	-	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 localization to extracellular region localization secretion by cell protein transport cellular macromolecule localization 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 localization to extracellular region localization secretion by cell protein transport cellular macromolecule localization macromolecule localization cellular process	cell periphery cell outer membrane cellular anatomical structure external encapsulating structure membrane cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR006182	Flagellar M-ring, N-terminal	Domain
A, B, C, D	IPR043427	Lipoprotein YscJ/Flagellar M-ring protein	Family
A, B, C, D	IPR003282	Type III secretion system lipoprotein SctJ	Family

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.