4N31

Structure and activity of Streptococcus pyogenes SipA: a signal peptidase homologue essential for pilus polymerisation

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	Peptidase_S24_1	e4n31A1	A: beta barrels	X: SH3	H: LexA/Signal peptidase (From Topology)	T: LexA/Signal peptidase	F: Peptidase_S24_1	ECOD (1.6)
B	Peptidase_S24_1	e4n31B1	A: beta barrels	X: SH3	H: LexA/Signal peptidase (From Topology)	T: LexA/Signal peptidase	F: Peptidase_S24_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.10.109.10	Mainly Beta	Ribbon	Umud Fragment, subunit A	Umud Fragment, subunit A	CATH (4.3.0)
B	2.10.109.10	Mainly Beta	Ribbon	Umud Fragment, subunit A	Umud Fragment, subunit A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF10502	Signal peptidase, peptidase S26 (Peptidase_S26)	Signal peptidase, peptidase S26	This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesised secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The ...	This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesised secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	SipA	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity	cellular biosynthetic process cellular metabolic process signal peptide processing primary metabolic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process proteolysis protein processing metabolic process cellular process protein metabolic process macromolecule metabolic process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR019533	Peptidase S26	Domain
A, B	IPR036286	LexA/Signal peptidase-like superfamily	Homologous Superfamily
A, B	IPR000223	Peptidase S26A, signal peptidase I	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.