P0ABU9: Tol-Pal system protein TolQ (tolQ)

Tol-Pal system protein TolQ (tolQ) is a 230-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0ABU9.

Gene
tolQ
Organism
Escherichia coli (strain K12)
Length
230 residues
Mean pLDDT
91.8
Model
AF-P0ABU9-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.8 (very high 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 accurate76%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825). Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction (PubMed:11722743). The Tol-Pal system is also required for polar localization of chemoreceptors clusters (PubMed:24720726). The system also appears to be required for the activity of several outer membrane-localized enzymes with cell wall remodeling activity (PubMed:32152098). Is involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA…

Subunit structure

The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer (PubMed:17233825). TolQ interacts with the N-terminal domain of TolA and with TolR (PubMed:10419942, PubMed:7744737)

Subcellular location

Cell inner membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9O40EM2.92 ÅA/B/C/D/E=1-230
9DDMEM2.94 ÅA/B/C/D/E=1-230
9DDNEM3.18 ÅA/B/C/D/E=1-230
9KPZEM3.18 ÅA/B/C/D/E=2-230
9QUQEM3.28 ÅA/B/C/D/E=1-230
9QVDEM3.52 ÅA/B/C/D/E=1-230
9K49EM3.6 ÅA/B/C/D/E=1-230
9KQ0EM3.6 ÅA/B/C/D/E=2-230
9KCHEM4.19 ÅA/B/C/D/E=1-230
8ODTEM4.2 ÅA/B/C/D/E=1-230

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