4CU9

Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA

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	F5_F8_type_C_like	e4cu9A1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: F5_F8_type_C_like	ECOD (1.6)
B	F5_F8_type_C_like	e4cu9B1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: F5_F8_type_C_like	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
B	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF21606	Beta-galactosidase-like, Galactose-binding domain (BgaA-like_CBM)	Beta-galactosidase-like, Galactose-binding domain	This domain is found in Beta-galactosidase from Streptococcus pneumoniae (BgaA) and similar bacterial sequences. BgaA is specific for terminal galactose residues beta-1-4 linked to glucose or N-acetylglucosamine. It is involved in pneumococcal growth ...	This domain is found in Beta-galactosidase from Streptococcus pneumoniae (BgaA) and similar bacterial sequences. BgaA is specific for terminal galactose residues beta-1-4 linked to glucose or N-acetylglucosamine. It is involved in pneumococcal growth, resistance to opsonophagocytic killing, and adherence. This entry represents two non-enzymatic carbohydrate-binding modules (CBMs) that mediate adherence to the host cell surface displayed lactose or N-acetyllactosamine. Each of these CBMs folds into a beta-sandwich fold comprising opposing sheets of 4- and 5-antiparallel beta-strands [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	BETA-GALACTOSIDASE	hydrolase activity, acting on glycosyl bonds beta-galactosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity galactosidase activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process primary metabolic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR032311	Domain of unknown function DUF4982	Domain
A, B	IPR051913	Glycosyl Hydrolase 2 Domain-Containing Protein	Family
A, B	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B	IPR006101	Glycoside hydrolase, family 2	Family
A, B	IPR040605	Glycoside hydrolase family 2, domain 5	Domain
A, B	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A, B	IPR006102	Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich	Domain
A, B	IPR036156	Beta-Galactosidase/glucuronidase domain superfamily	Homologous Superfamily
A, B	IPR006104	Glycosyl hydrolases family 2, sugar binding domain	Domain
A, B	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A, B	IPR005877	YSIRK Gram-positive signal peptide	Domain
A, B	IPR011098	G5 domain	Domain
A, B	IPR006103	Glycoside hydrolase family 2, catalytic domain	Domain
A, B	IPR049487	Beta-galactosidase-like, galactose-binding domain	Domain
A, B	IPR011081	Bacterial Ig-like domain	Domain
A, B	IPR019931	LPXTG cell wall anchor domain	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 R01GM157729.