6VC7

Structure of the F349A mutant of the periplasmic domain of YejM from Salmonella typhimurium

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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	SCOP2B Superfamily	Alkaline phosphatase-like	8092296	3001353	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Arylsulfatase, C-terminal domain-like	8092298	3002305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Alkaline phosphatase-like	8092296	3001353	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Arylsulfatase, C-terminal domain-like	8092298	3002305	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Alkaline phosphatase-like	8092296	3001353	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Arylsulfatase, C-terminal domain-like	8092298	3002305	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Alkaline phosphatase-like	8092296	3001353	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Arylsulfatase, C-terminal domain-like	8092298	3002305	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Alkaline phosphatase-like	8092296	3001353	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Arylsulfatase, C-terminal domain-like	8092298	3002305	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Alkaline phosphatase-like	8092296	3001353	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Arylsulfatase, C-terminal domain-like	8092298	3002305	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	Sulfatase_1	e6vc7A1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Sulfatase_1	ECOD (1.6)
B	Sulfatase_1	e6vc7B1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Sulfatase_1	ECOD (1.6)
C	Sulfatase_1	e6vc7C1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Sulfatase_1	ECOD (1.6)
D	Sulfatase_1	e6vc7D1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Sulfatase_1	ECOD (1.6)
E	Sulfatase_1	e6vc7E1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Sulfatase_1	ECOD (1.6)
F	Sulfatase_1	e6vc7F1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Sulfatase_1	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	PF00884	Sulfatase (Sulfatase)	Sulfatase	-	Family

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	Periplasmic domain of the cardiolipin transporter protein YejM/PbgA	-	-	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR000917	Sulfatase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR012159	Inner membrane protein YejM-like	Family
A, B, C, D, E A, B, C, D, E, F	IPR047997	Inner membrane protein YejM, enterobacterales	Family
A, B, C, D, E A, B, C, D, E, F	IPR024588	Inner membrane protein YejM, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR017850	Alkaline-phosphatase-like, core domain 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.