Q9A5I5 · PLED_CAUVC
- ProteinResponse regulator PleD
- GenepleD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids454 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition.
Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger.
Catalytic activity
- 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Activity regulation
Allosterically inhibited by the product c-di-GMP.
Pathway
Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 10 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 53 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 55 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Site | 178 | Allosteric product binding | ||||
Sequence: R | ||||||
Site | 332 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 335 | substrate | ||||
Sequence: N | ||||||
Binding site | 344 | substrate | ||||
Sequence: D | ||||||
Site | 359 | Allosteric product phosphate group binding | ||||
Sequence: R | ||||||
Site | 362 | Allosteric product binding | ||||
Sequence: D | ||||||
Active site | 370 | Proton acceptor | ||||
Sequence: E | ||||||
Site | 390 | Allosteric product binding | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | diguanylate cyclase activity | |
Molecular Function | GTP binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Biological Process | cell adhesion involved in single-species biofilm formation | |
Biological Process | cell differentiation | |
Biological Process | negative regulation of bacterial-type flagellum-dependent cell motility | |
Biological Process | phosphorelay signal transduction system |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameResponse regulator PleD
- Alternative names
Including 1 domain:
- Recommended nameDiguanylate cyclase
- EC number
- Short namesDGC
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Caulobacterales > Caulobacteraceae > Caulobacter
Accessions
- Primary accessionQ9A5I5
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Phosphorylated PleD localizes to the differentiating pole.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000081206 | 1-454 | Response regulator PleD | |||
Sequence: MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDPVSALLIDIDFFKKINDTFGHDIGDEVLREFALRLASNVRAIDLPCRYGGEEFVVIMPDTALADALRIAERIRMHVSGSPFTVAHGREMLNVTISIGVSATAGEGDTPEALLKRADEGVYQAKASGRNAVVGKAA | ||||||
Modified residue | 53 | 4-aspartylphosphate | ||||
Sequence: D |
Post-translational modification
Phosphorylated by PleC and DivJ. Phosphorylation stimulates cyclase activity (By similarity).
Keywords
- PTM
Interaction
Subunit
Homodimer. Inactive monomer in solution (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9A5I5 | divJ Q03228 | 3 | EBI-1784732, EBI-1785038 | |
BINARY | Q9A5I5 | pleC P37894 | 4 | EBI-1784732, EBI-1784742 | |
BINARY | Q9A5I5 | pleD Q9A5I5 | 4 | EBI-1784732, EBI-1784732 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-120 | Response regulatory 1 | ||||
Sequence: RILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLT | ||||||
Domain | 155-269 | Response regulatory 2 | ||||
Sequence: RVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQI | ||||||
Domain | 319-454 | GGDEF | ||||
Sequence: DPVSALLIDIDFFKKINDTFGHDIGDEVLREFALRLASNVRAIDLPCRYGGEEFVVIMPDTALADALRIAERIRMHVSGSPFTVAHGREMLNVTISIGVSATAGEGDTPEALLKRADEGVYQAKASGRNAVVGKAA |
Domain
Activated by phosphorylation at the first response regulatory domain, which induces dimerization mediated by the two response regulatory domains and allows the two substrate-binding sites to approach each other and the condensation reaction to occur (Probable). The diguanylate cyclase activity is harbored by the GGDEF domain (By similarity).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length454
- Mass (Da)49,624
- Last updated2001-06-01 v1
- ChecksumD44909D42B581516
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 45-48 | in Ref. 1; AAA87378 | ||||
Sequence: DLPD → ICPT | ||||||
Sequence conflict | 274 | in Ref. 1; AAA87378 | ||||
Sequence: Y → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L42554 EMBL· GenBank· DDBJ | AAA87378.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE005673 EMBL· GenBank· DDBJ | AAK24433.1 EMBL· GenBank· DDBJ | Genomic DNA |