Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

papD (P15319) - Overview - Molecular Target Synopsis

Protein


papD, Chaperone protein PapD
UniProt P15319

Also Known as PAPD_ECOLX, papD

Binds and caps interactive surfaces on P pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of P pilus subunits into the periplasm, probably also facilitates their folding (PubMed:9351822). Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits. Coexpression of this chaperone with individual, otherwise toxic, P pilus subunits (tested with PapA, PapE and PapG) suppresses their growth inhibitory phenotype (PubMed:9351822). Interacts with substrates PapG and PapK.

6CD2
CRYSTAL STRUCTURE OF THE PAPC USHER BOUND TO THE CHAPERONE-ADHESIN PAPD-PAPG
RCSB/PDB
Inspect Structure
See all 3D Structures for papD

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
239P15319-1

Sub-cellular localization


UniProt: papD is active in the following subcellular-locations: periplasm.
GO terms: papD is active in the following subcellular-locations: outer membrane-bounded periplasmic space.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project papD has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For papD there are:
10 structures (14 chains) solved
2 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


papD has been screened with 18 compounds (18 bioactivities). (see details)