Bacillus Subtilis Phosphotransferase System Activity on Rifampicin

Šárka Bobková's 2026 supplementary document provides biochemical evidence linking the bacterial phosphotransferase system (PTS) to rifampicin inactivation. The 881.4 KB file details in vitro and in vivo assays with Bacillus subtilis strains, identifying protein EI's phosphorylation capability. It establishes RphT as a functional rifampicin-modifying enzyme and explores evolutionary connections to antibiotic resistance mechanisms.

Use Cases

• Analyze the homology between PTS protein sequences and rifampicin phosphotransferases (RPHs) to study enzyme evolution.
• Train models to predict rifampicin resistance from genetic features like ptsH, ptsI, or rphT gene presence/absence in Bacillus subtilis.
• Use growth assay results under rifampicin exposure to benchmark the phenotypic impact of specific gene deletions.
• Correlate in vitro phosphorylation assay outcomes with protein interaction data from thermophoresis experiments to validate enzyme activity.

Strengths

• Data is recent, with a last update in April 2026.
• Provides direct biochemical evidence for a previously hypothesized evolutionary link between protein systems.
• Includes results from multiple experimental methods: growth assays, liquid chromatography-mass spectrometry, and thermophoresis.

Limitations

• The dataset is very small at 881.4 KB, containing a single supplementary document rather than a structured data table.
• Scope is limited to specific Bacillus subtilis strains and proteins (EI, HPr, MtlF, PckA, RphT), limiting generalizability.
• No raw numerical data or columnar datasets are provided; analysis requires extracting information from textual descriptions.

Provenance

Source

figshare, authored by Šárka Bobková.

Collection Method

Experimental data from bacterial growth assays, in vitro phosphorylation assays using liquid chromatography-mass spectrometry, and protein–ligand interaction analysis via thermophoresis.

Freshness

Last updated on 2026-04-08.