4ZVG

Crystal structure of GGDEF domain of the E. coli DosC - form III

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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8098390	3001272	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8098390	3001272	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	GGDEF	e4zvgA1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: GGDEF	ECOD (1.6)
B	GGDEF	e4zvgB1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: GGDEF	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.270	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Reverse transcriptase/Diguanylate cyclase domain	CATH (4.3.0)
B	3.30.70.270	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Reverse transcriptase/Diguanylate cyclase domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00990	Diguanylate cyclase, GGDEF domain (GGDEF)	Diguanylate cyclase, GGDEF domain	This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain [1] and has diguanylate cyclase activity [4]. This observation correlates with ...	This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain [1] and has diguanylate cyclase activity [4]. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyses the cyclisation of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule [6,7,8].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Diguanylate cyclase DosC	oxygen binding binding small molecule binding transferase activity nucleotidyltransferase activity catalytic activity diguanylate cyclase activity transferase activity, transferring phosphorus-containing groups identical protein binding protein binding protein homodimerization activity protein dimerization activity organic cyclic compound binding tetrapyrrole binding oxygen binding binding small molecule binding transferase activity nucleotidyltransferase activity catalytic activity diguanylate cyclase activity transferase activity, transferring phosphorus-containing groups identical protein binding protein binding protein homodimerization activity protein dimerization activity organic cyclic compound binding tetrapyrrole binding heme binding carbon monoxide binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding cation binding metal ion binding	response to stimulus response to stress regulation of bacterial-type flagellum-dependent cell motility negative regulation of locomotion regulation of biological process regulation of cell motility regulation of cellular process biological regulation negative regulation of biological process archaeal or bacterial-type flagellum-dependent cell motility cilium or flagellum-dependent cell motility regulation of locomotion negative regulation of cellular process negative regulation of cell motility response to stimulus response to stress regulation of bacterial-type flagellum-dependent cell motility negative regulation of locomotion regulation of biological process regulation of cell motility regulation of cellular process biological regulation negative regulation of biological process archaeal or bacterial-type flagellum-dependent cell motility cilium or flagellum-dependent cell motility regulation of locomotion negative regulation of cellular process negative regulation of cell motility cellular process bacterial-type flagellum-dependent cell motility cell motility negative regulation of bacterial-type flagellum-dependent cell motility locomotion response to oxygen levels response to abiotic stimulus cell adhesion involved in biofilm formation cell aggregation biofilm formation biological process involved in intraspecies interaction between organisms cell-substrate adhesion single-species biofilm formation aggregation of unicellular organisms submerged biofilm formation cell adhesion involved in single-species biofilm formation cell adhesion single-species submerged biofilm formation	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR050469	Bacterial Diguanylate Cyclase	Family
A, B	IPR000160	GGDEF domain	Domain
A, B	IPR009050	Globin-like superfamily	Homologous Superfamily
A, B	IPR043128	Reverse transcriptase/Diguanylate cyclase domain	Homologous Superfamily
A, B	IPR012292	Globin/Protoglobin	Homologous Superfamily
A, B	IPR044398	Globin-sensor domain	Domain
A, B	IPR048442	DosC, CZB-like middle domain	Domain
A, B	IPR039435	Diguanylate cyclase DosC, globin sensor domain	Domain
A, B	IPR029787	Nucleotide cyclase	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.