Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA0993
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: cupC2 PA0993
Status: annotated
Amino acids: 237
Structure source: AlphaFold

GO

GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. GO:0044183 Binding to a protein or a protein-containing complex to assist the protein folding process. GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies. GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Periplasmic

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5

GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:0044183 Binding to a protein or a protein-containing complex to assist the protein folding process.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies.
GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.

Sequence Features

Domain/signature hits from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
135	232	SUPERFAMILY	SSF49584	Periplasmic chaperone C-domain
135	232	InterPro	IPR036316	Pili assembly chaperone, C-terminal domain superfamily
20	24	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	24	SignalP_EUK	SignalP-TM	SignalP-TM
20	141	SUPERFAMILY	SSF49354	PapD-like
20	141	InterPro	IPR008962	PapD-like superfamily
9	19	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	24	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	8	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
145	237	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
145	237	InterPro	IPR013783	Immunoglobulin-like fold
25	141	Pfam	PF00345	Pili and flagellar-assembly chaperone, PapD N-terminal domain
25	141	InterPro	IPR016147	Pili assembly chaperone, N-terminal
9	31	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
25	142	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
25	142	InterPro	IPR013783	Immunoglobulin-like fold
167	229	Pfam	PF02753	Pili assembly chaperone PapD, C-terminal domain
167	229	InterPro	IPR016148	Pili assembly chaperone, C-terminal
25	237	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
123	138	PRINTS	PR00969	Pili chaperone signature
123	138	InterPro	IPR001829	Pili assembly chaperone, bacterial
162	177	PRINTS	PR00969	Pili chaperone signature
162	177	InterPro	IPR001829	Pili assembly chaperone, bacterial
72	93	PRINTS	PR00969	Pili chaperone signature
72	93	InterPro	IPR001829	Pili assembly chaperone, bacterial
26	35	PRINTS	PR00969	Pili chaperone signature
26	35	InterPro	IPR001829	Pili assembly chaperone, bacterial
100	117	PRINTS	PR00969	Pili chaperone signature
100	117	InterPro	IPR001829	Pili assembly chaperone, bacterial
8	235	PANTHER	PTHR30251	PILUS ASSEMBLY CHAPERONE

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

No pockets are loaded yet for the displayed AlphaFold model PA0993 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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Structural evidence

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA0993	AlphaFold	—	—	full sequence	—	Viewing

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

3 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
EC2	2XG5	P15319	453.6 Da LogP 5.94 TPSA 59.3	1 viol.	✓ Clean	`c1ccc(cc1)[C@@H]2[C@H](N3C(=O)C=C(C(=C3S2)C4CC4…`
EC5	2XG5	P15319	471.6 Da LogP 5.90 TPSA 79.5	1 viol.	✓ Clean	`c1ccc(cc1)C[C@@H](C(=O)O)N2C(=O)C=C(C(=C2SO)C3C…`
XC2	2XG4	P15319	476.6 Da LogP 4.03 TPSA 71.8	✓ Ro5	✓ Clean	`c1ccc2c(c1)cccc2CC3=C(C(=O)N4[C@@H](CSC4=C3C5CC…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.