Q9A5I5 · PLED_CAUVC

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

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.

TypeIDPosition(s)Description
Binding site9Mg2+ (UniProtKB | ChEBI)
Binding site10Mg2+ (UniProtKB | ChEBI)
Binding site53Mg2+ (UniProtKB | ChEBI)
Binding site55Mg2+ (UniProtKB | ChEBI)
Site178Allosteric product binding
Site332Transition state stabilizer
Binding site335substrate
Binding site344substrate
Site359Allosteric product phosphate group binding
Site362Allosteric product binding
Active site370Proton acceptor
Site390Allosteric product binding

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular Functiondiguanylate cyclase activity
Molecular FunctionGTP binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Biological Processcell adhesion involved in single-species biofilm formation
Biological Processcell differentiation
Biological Processnegative regulation of bacterial-type flagellum-dependent cell motility
Biological Processphosphorelay signal transduction system

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Response regulator PleD
  • Alternative names
    • Stalked cell differentiation-controlling protein

Including 1 domain:

  • Recommended name
    Diguanylate cyclase
  • EC number
  • Short names
    DGC
  • Alternative names
    • Diguanylate kinase

Gene names

    • Name
      pleD
    • Ordered locus names
      CC_2462

Organism names

Accessions

  • Primary accession
    Q9A5I5
  • Secondary accessions
    • Q46020

Proteomes

Subcellular Location

Cytoplasm
Note: Phosphorylated PleD localizes to the differentiating pole.

Keywords

Phenotypes & Variants

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000812061-454Response regulator PleD
Modified residue534-aspartylphosphate

Post-translational modification

Phosphorylated by PleC and DivJ. Phosphorylation stimulates cyclase activity (By similarity).

Keywords

Interaction

Subunit

Homodimer. Inactive monomer in solution (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9A5I5divJ Q032283EBI-1784732, EBI-1785038
BINARY Q9A5I5pleC P378944EBI-1784732, EBI-1784742
BINARY Q9A5I5pleD Q9A5I54EBI-1784732, EBI-1784732

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-120Response regulatory 1
Domain155-269Response regulatory 2
Domain319-454GGDEF

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    454
  • Mass (Da)
    49,624
  • Last updated
    2001-06-01 v1
  • Checksum
    D44909D42B581516
MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDPVSALLIDIDFFKKINDTFGHDIGDEVLREFALRLASNVRAIDLPCRYGGEEFVVIMPDTALADALRIAERIRMHVSGSPFTVAHGREMLNVTISIGVSATAGEGDTPEALLKRADEGVYQAKASGRNAVVGKAA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict45-48in Ref. 1; AAA87378
Sequence conflict274in Ref. 1; AAA87378

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L42554
EMBL· GenBank· DDBJ
AAA87378.1
EMBL· GenBank· DDBJ
Genomic DNA
AE005673
EMBL· GenBank· DDBJ
AAK24433.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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