3KXY

Crystal Structure of the ExsC-ExsE Complex

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	PF05932	e3kxyA1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
B	PF05932	e3kxyB1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
D [auth C]	PF05932	e3kxyC1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
E [auth D]	PF05932	e3kxyD1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
H [auth F]	PF05932	e3kxyF1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
K [auth H]	PF05932	e3kxyH1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
M [auth I]	PF05932	e3kxyI1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
N [auth J]	PF05932	e3kxyJ1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
Q [auth L]	PF05932	e3kxyL1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
G [auth E]	PF05932	e3kxyE1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
J [auth G]	PF05932	e3kxyG1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
P [auth K]	PF05932	e3kxyK1	A: a+b two layers	X: Type III secretory system chaperone-like	H: Type III secretory system chaperone (From Topology)	T: Type III secretory system chaperone	F: PF05932	ECOD (1.6)
C [auth T]	PF18286	e3kxyT1	A: extended segments	X: ExsE (From Topology)	H: ExsE (From Topology)	T: ExsE	F: PF18286	ECOD (1.6)
F [auth U]	PF18286	e3kxyU1	A: extended segments	X: ExsE (From Topology)	H: ExsE (From Topology)	T: ExsE	F: PF18286	ECOD (1.6)
I [auth V]	PF18286	e3kxyV1	A: extended segments	X: ExsE (From Topology)	H: ExsE (From Topology)	T: ExsE	F: PF18286	ECOD (1.6)
L [auth W]	F_UNCLASSIFIED	e3kxyW1	A: extended segments	X: ExsE (From Topology)	H: ExsE (From Topology)	T: ExsE	F: F_UNCLASSIFIED	ECOD (1.6)
R [auth Y]	PF18286	e3kxyY1	A: extended segments	X: ExsE (From Topology)	H: ExsE (From Topology)	T: ExsE	F: PF18286	ECOD (1.6)
O [auth X]	F_UNCLASSIFIED	e3kxyX1	A: extended segments	X: ExsE (From Topology)	H: ExsE (From Topology)	T: ExsE	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
B	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
D [auth C]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
E [auth D]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
H [auth F]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
K [auth H]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
M [auth I]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
N [auth J]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
Q [auth L]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
G [auth E]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
J [auth G]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
P [auth K]	3.30.1460.10	Alpha Beta	2-Layer Sandwich	Yope Regulator	Chain: A,	CATH (4.3.0)
C [auth T]	6.20.290.10	Special	Other non-globular	Dna Ligase	domain 1	CATH (4.3.0)
F [auth U]	6.20.290.10	Special	Other non-globular	Dna Ligase	domain 1	CATH (4.3.0)
I [auth V]	6.20.290.10	Special	Other non-globular	Dna Ligase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F], J [auth G], K [auth H], M [auth I], N [auth J], P [auth K], Q [auth L]	PF05932	Tir chaperone protein (CesT) family (CesT)	Tir chaperone protein (CesT) family	This family consists of a number of bacterial sequences which are highly similar to the Tir chaperone protein in E. Coli. In many Gram-negative bacteria, a key indicator of pathogenic potential is the possession of a specialised type III secretion sy ...	This family consists of a number of bacterial sequences which are highly similar to the Tir chaperone protein in E. Coli. In many Gram-negative bacteria, a key indicator of pathogenic potential is the possession of a specialised type III secretion system, which is utilised to deliver virulence effector proteins directly into the host cell cytosol. Many of the proteins secreted from such systems require small cytosolic chaperones to maintain the secreted substrates in a secretion-competent state. CesT serves a chaperone function for the enteropathogenic Escherichia coli (EPEC) translocated intimin receptor (Tir) protein, which confers upon EPEC the ability to alter host cell morphology following intimate bacterial attachment [1]. This family also contains several DspF and related sequences from several plant pathogenic bacteria. The "disease-specific" (dsp) region next to the hrp gene cluster of Erwinia amylovora is required for pathogenicity but not for elicitation of the hypersensitive reaction. DspF and AvrF are small (16 kDa and 14 kDa) and acidic with predicted amphipathic alpha helices in their C termini; they resemble chaperones for virulence factors secreted by type III secretion systems of animal pathogens [2].	Domain
C [auth T], F [auth U], I [auth V], L [auth W], O [auth X], C [auth T], F [auth U], I [auth V], L [auth W], O [auth X], R [auth Y]	PF18286	Type III secretion system ExsE (T3SS_ExsE)	Type III secretion system ExsE	This domain is found in ExsE present in Pseudomonas aeruginosa. ExsE forms part of the ExsACDE signaling cascade which acts as an important regulatory switch that ensures timely expression of the Type III secretion system (T3SS) and so plays a critic ...	This domain is found in ExsE present in Pseudomonas aeruginosa. ExsE forms part of the ExsACDE signaling cascade which acts as an important regulatory switch that ensures timely expression of the Type III secretion system (T3SS) and so plays a critical role in facilitating infection. Prior to host-cell contact, the T3SS is inactive and ExsE and Type III Secretion Chaperone (ExsC) form a stable complex. ExsC forms a compact homodimer and ExsE wraps around one face of this dimer [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F], J [auth G], K [auth H], M [auth I], N [auth J], P [auth K], Q [auth L]	Exoenzyme S synthesis protein C	-	regulation of cellular process positive regulation of macromolecule biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process positive regulation of metabolic process DNA-templated transcription regulation of RNA metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process regulation of biological process positive regulation of nucleobase-containing compound metabolic process cellular metabolic process primary metabolic process regulation of cellular process positive regulation of macromolecule biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process positive regulation of metabolic process DNA-templated transcription regulation of RNA metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process regulation of biological process positive regulation of nucleobase-containing compound metabolic process cellular metabolic process primary metabolic process regulation of cellular metabolic process positive regulation of RNA metabolic process organic cyclic compound metabolic process regulation of gene expression biosynthetic process organic cyclic compound biosynthetic process metabolic process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process positive regulation of DNA-templated transcription cellular biosynthetic process positive regulation of biological process RNA metabolic process positive regulation of cellular metabolic process RNA biosynthetic process nucleic acid biosynthetic process organic substance metabolic process positive regulation of biosynthetic process positive regulation of cellular process regulation of RNA biosynthetic process regulation of biosynthetic process biological regulation regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of cellular biosynthetic process positive regulation of RNA biosynthetic process cellular process positive regulation of cellular biosynthetic process protein localization establishment of protein localization cellular localization nitrogen compound transport transport secretion organic substance transport protein secretion by the type III secretion system establishment of protein localization to extracellular region export from cell protein secretion establishment of localization protein localization to extracellular region transmembrane transport localization secretion by cell protein transmembrane transport protein transport cellular macromolecule localization macromolecule localization	intracellular anatomical structure cytoplasm cellular anatomical entity
C [auth T], F [auth U], I [auth V], L [auth W], O [auth X], C [auth T], F [auth U], I [auth V], L [auth W], O [auth X], R [auth Y]	ExsE	protein binding binding protein-folding chaperone binding	negative regulation of protein transport protein localization regulation of localization establishment of protein localization cellular localization nitrogen compound transport regulation of cellular process regulation of protein localization transport negative regulation of biological process negative regulation of transport protein localization to extracellular region localization negative regulation of secretion regulation of secretion by cell negative regulation of protein transport protein localization regulation of localization establishment of protein localization cellular localization nitrogen compound transport regulation of cellular process regulation of protein localization transport negative regulation of biological process negative regulation of transport protein localization to extracellular region localization negative regulation of secretion regulation of secretion by cell secretion by cell cellular macromolecule localization negative regulation of cellular process negative regulation of secretion by cell negative regulation of protein localization regulation of biological process regulation of transport secretion organic substance transport biological regulation regulation of establishment of protein localization establishment of protein localization to extracellular region negative regulation of establishment of protein localization export from cell regulation of protein transport protein secretion establishment of localization regulation of secretion regulation of protein secretion negative regulation of protein secretion protein transport regulation of cellular localization macromolecule localization cellular process cellular response to stimulus cellular response to inorganic substance cellular response to metal ion response to stimulus response to inorganic substance cellular response to chemical stimulus response to metal ion response to chemical cellular response to calcium ion response to calcium ion protein secretion by the type III secretion system transmembrane transport protein transmembrane transport	intracellular anatomical structure cytoplasm cellular anatomical entity extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F], J [auth G], K [auth H], M [auth I], N [auth J], P [auth K], Q [auth L]	IPR010261	Tir chaperone protein (CesT) family	Family
C [auth T], F [auth U], I [auth V], L [auth W], O [auth X], C [auth T], F [auth U], I [auth V], L [auth W], O [auth X], R [auth Y]	IPR040866	Type III secretion system ExsE	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 R01GM133198.