4P00

Bacterial Cellulose Synthase in complex with cyclic-di-GMP and UDP

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
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	BcsA TM domain-like	8091602	3002523	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	PilZ domain-like	8091599	3000480	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Nucleotide-diphospho-sugar transferases	8091601	3000077	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	BcsA TM domain-like	8091602	3002523	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	PilZ	e4p00A2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel	F: PilZ	ECOD (1.6)
A	Glyco_tranf_2_3	e4p00A3	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: Glyco_tranf_2_3	ECOD (1.6)
B	BcsB_1st	e4p00B3	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: BcsB_1st	ECOD (1.6)
B	BcsB_2nd	e4p00B1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: BcsB_2nd	ECOD (1.6)
B	EUF08642	e4p00B2	A: a/b three-layered sandwiches	X: Cellulose Synthase Subunit B a/b domain (From Topology)	H: Cellulose Synthase Subunit B a/b domain (From Topology)	T: Cellulose Synthase Subunit B a/b domain	F: EUF08642	ECOD (1.6)
B	EUF08643	e4p00B4	A: a/b three-layered sandwiches	X: Cellulose Synthase Subunit B a/b domain (From Topology)	H: Cellulose Synthase Subunit B a/b domain (From Topology)	T: Cellulose Synthase Subunit B a/b domain	F: EUF08643	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
A	2.40.10.220	Mainly Beta	Beta Barrel	Thrombin, subunit H	predicted glycosyltransferase like domains	CATH (4.3.0)
B	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
B	3.30.379.20	Alpha Beta	2-Layer Sandwich	Chitobiase	domain 2	CATH (4.3.0)
B	3.30.379.30	Alpha Beta	2-Layer Sandwich	Chitobiase	domain 2	CATH (4.3.0)
B	1.20.5.4520	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF07238	PilZ domain (PilZ)	PilZ domain	PilZ is a c-di-GMP binding domain [3] found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, ...	PilZ is a c-di-GMP binding domain [3] found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP [6]. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias [5]. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix [6].	Domain
A	PF13641	Glycosyltransferase like family 2 (Glyco_tranf_2_3)	Glycosyltransferase like family 2	Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis [1][2].	Domain
B	PF03170	Bacterial cellulose synthase subunit (BcsB)	Bacterial cellulose synthase subunit	-	Family
B	PF20916	Cellulose Synthase Subunit B, alpha-beta domain (BscB_a-b)	Cellulose Synthase Subunit B, alpha-beta domain	This domain is found in Cellulose Synthase Subunit B (BscB) from Cereibacter sphaeroides and similar sequences predominantly found in bacteria. BscB, involved in bacterial cellulose biosynthesis, is organized into two periplasmic carbohydrate binding ...	This domain is found in Cellulose Synthase Subunit B (BscB) from Cereibacter sphaeroides and similar sequences predominantly found in bacteria. BscB, involved in bacterial cellulose biosynthesis, is organized into two periplasmic carbohydrate binding domains (CBD-1/2, Pfam:PF03170) and two alpha/beta-domains with similarity with a flavodoxin-fold (FD1 and FD2) [1]. This entry represents FD2.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Cellulose Synthase A subunit	guanyl nucleotide binding binding cyclic nucleotide binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding cyclic-di-GMP binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding guanyl nucleotide binding binding cyclic nucleotide binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding cyclic-di-GMP binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding UDP-glycosyltransferase activity glycosyltransferase activity cellulose synthase (UDP-forming) activity cellulose synthase activity transferase activity glucosyltransferase activity hexosyltransferase activity catalytic activity UDP-glucosyltransferase activity	nucleoside phosphate metabolic process UDP-alpha-D-glucose metabolic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process carbohydrate metabolic process nucleoside phosphate metabolic process UDP-alpha-D-glucose metabolic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process carbohydrate metabolic process glucan biosynthetic process beta-glucan metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process macromolecule biosynthetic process beta-glucan biosynthetic process polysaccharide metabolic process glucan metabolic process biosynthetic process cellulose biosynthetic process macromolecule metabolic process cellulose metabolic process	cell periphery cellular anatomical structure plasma membrane membrane
B	Cellulose Synthase B subunit	cation binding ion binding binding metal ion binding small molecule binding	nucleoside phosphate metabolic process UDP-alpha-D-glucose metabolic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process carbohydrate metabolic process nucleoside phosphate metabolic process UDP-alpha-D-glucose metabolic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process carbohydrate metabolic process glucan biosynthetic process beta-glucan metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process macromolecule biosynthetic process beta-glucan biosynthetic process polysaccharide metabolic process glucan metabolic process biosynthetic process cellulose biosynthetic process macromolecule metabolic process cellulose metabolic process	cell periphery cellular anatomical structure plasma membrane membrane
C [auth D]	unidentified peptide	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR003919	Cellulose synthase, subunit A	Family
A	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily
A	IPR050321	Glycosyltransferase 2/OpgH subfamily	Family
A	IPR009875	PilZ domain	Domain
B	IPR018513	Cellulose synthase BcsB, bacterial	Family
B	IPR048861	Cellulose synthase subunit B-like, C-terminal domain	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM	Transmembrane	Alpha-helical polytopic	Glycosyl transferase/transporter	Glycan glucosyl transferase

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B	MemProtMD	Annotated as membrane protein by MemProtMD

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.