Protein profile

PA5134

carboxyl-terminal protease

Genome: NC_002516.2

Gene: PA5134 Structure source: Experimental + AlphaFold UniProt Q9HU50

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Amino acids 436

Annotations 13

Features 37

PDB binders 1

Druggability 0.926

Overview

Basic information about this protein and its source genome.

Accession: PA5134
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5134
Status: annotated
Amino acids: 436
Structure source: Experimental + AlphaFold

GO:0030313 An envelope that surrounds a bacterial cell and includes the cytoplasmic membrane and everything external, encompassing the periplasmic space, cell wall, and outer membrane if present. 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:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

Target profile

Computed evidence for target prioritization.

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

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.926

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

GO:0030313 An envelope that surrounds a bacterial cell and includes the cytoplasmic membrane and everything external, encompassing the periplasmic space, cell wall, and outer membrane if present.
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:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0043163 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cell envelope, everything external to, but not including, the cytoplasmic membrane of bacteria, encompassing the periplasmic space, cell wall, and outer membrane if present.
GO:0042546 A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a cell wall. Includes biosynthesis of constituent macromolecules, such as proteins and polysaccharides, and those macromolecular modifications that are involved in synthesis or assembly of the cellular component. A cell wall is 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:0030254 The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0005515 Binding to a protein.

Sequence Features

Domain/signature hits from InterPro and related databases.

37 records

Show feature table

Start	End	DB	Term	Name
54	113	FunFam	G3DSA:3.30.750.44:FF:000001	S41 family peptidase
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
8	18	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
104	188	CDD	cd00988	PDZ_CTP_protease
105	191	Gene3D	G3DSA:2.30.42.10	-
105	191	InterPro	IPR036034	PDZ superfamily
24	436	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
59	376	NCBIfam	TIGR00225	C-terminal processing peptidase
59	376	InterPro	IPR004447	C-terminal-processing peptidase S41A
121	224	Pfam	PF02163	Peptidase family M50
121	224	InterPro	IPR008915	Peptidase M50
105	191	FunFam	G3DSA:2.30.42.10:FF:000063	Peptidase, S41 family
105	176	SMART	SM00228	pdz_new
105	176	InterPro	IPR001478	PDZ domain
19	23	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
177	369	SMART	SM00245	tsp_4
177	369	InterPro	IPR005151	Tail specific protease
1	23	SignalP_EUK	SignalP-noTM	SignalP-noTM
44	373	PANTHER	PTHR32060	TAIL-SPECIFIC PROTEASE
42	370	SUPERFAMILY	SSF52096	ClpP/crotonase
42	370	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
192	366	Gene3D	G3DSA:3.90.226.10	-
192	366	FunFam	G3DSA:3.90.226.10:FF:000029	Peptidase, S41 family
44	368	CDD	cd07560	Peptidase_S41_CPP
44	368	InterPro	IPR004447	C-terminal-processing peptidase S41A
389	420	MobiDBLite	mobidb-lite	consensus disorder prediction
97	178	SUPERFAMILY	SSF50156	PDZ domain-like
97	178	InterPro	IPR036034	PDZ superfamily
53	344	Gene3D	G3DSA:3.30.750.44	-
1	23	Phobius	SIGNAL_PEPTIDE	Signal peptide region
203	368	Pfam	PF03572	Peptidase family S41
203	368	InterPro	IPR005151	Tail specific protease
120	174	Pfam	PF17820	PDZ domain
120	174	InterPro	IPR041489	PDZ domain 6
1	23	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
93	161	ProSiteProfiles	PS50106	PDZ domain profile.
93	161	InterPro	IPR001478	PDZ domain

3D Structure

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

Loading 3D structure...

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Structural evidence

2 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 7RQH	X-ray	3.20 Å	A,B	91.3% 38-435	PDBe RCSB PDBj File	Viewing
PDB 7RPQ	X-ray	3.30 Å	A,B	91.5% 38-436	PDBe RCSB PDBj File	Loaded
AlphaFold PA5134	AlphaFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
3				0.926
5				0.785
1				0.224

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				1.22	0.011

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
4				0.906
13				0.7
7				0.216
2				0.212

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.

1 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
TMO	6VBB	A0A1E3M7A1	75.1 Da LogP 0.19 TPSA 23.1	✓ Ro5	✓ Clean	`C[N+](C)(C)[O-]`

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.