Q9I788: Exoenzyme T (exoT)

Exoenzyme T (exoT) is a 457-residue protein from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9I788.

Gene
exoT
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
457 residues
Mean pLDDT
77.4
Model
AF-Q9I788-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.4 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate50%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Bifunctional effector protein that is secreted and delivered by the type III secretion system into eukaryotic target cells. ADP-ribosylates several eukaryotic proteins including CT10 regulator of kinase (Crk) proteins (PubMed:12807879). In turn, induces atypical anoikis apoptosis by transforming Crk adaptor protein into a cytotoxin (PubMed:26020630). Affects host cell morphology by disrupting the actin cytoskeleton (PubMed:14688136). In addition to this activity, acts via its N-terminal region as a GTPase-activating protein (GAP) for host Rho GTPases including RhoA, Rac1, Cdc42 and Ras (PubMed:11895987). The bacterial Rho-GAP domain activity induces mitochondrial disruption in the target…

Subunit structure

Interacts with chaperone protein SpcS; this interaction maintains ExoT in a secretion competent state within the cytoplasm (PubMed:24387107). Interacts with host YWHAB (PubMed:30224724)

Subcellular location

Secreted

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
4JMFX-ray2.1 ÅA=28-77
6JNPX-ray2.26 ÅA/D=23-79
6GNNX-ray3.79 ÅC=235-457

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