thermophilic

METPO:1000616 · CLASS · REVIEWED

A temperature preference in which growth is favored at elevated temperatures, typically ≥45 °C.

Thermophilic heat-adaptation mechanism

Evidence-backed causal sketch linking thermophily to elevated temperature, membrane lipid adaptation, thermostable proteins, and energy transduction constraints.

Thermophilic heat-adaptation mechanism Interactive directed graph showing evidence-backed causal relationships for thermophilic.

Edge evidence

  • high temperature selects for thermophilic METPO:2007401

    High-temperature environments select for thermophilic growth capacity.

    • DOI:10.1016/s0300-9629(97)00003-0 adapted to environments of high temperature Review supports thermophile adaptation to high-temperature environments.
  • high temperature increases membrane proton permeability RO:0002213

    Elevated temperature increases proton permeability of the cytoplasmic membrane.

    • DOI:10.1016/s0300-9629(97)00003-0 proton permeability ... increase with the temperature Supports membrane proton permeability as a high-temperature growth constraint.
  • membrane lipid composition limits membrane proton permeability RO:0002212

    Lipid composition changes can reduce high-temperature membrane leakiness.

    • DOI:10.1016/s0300-9629(97)00003-0 changing the lipid composition Supports lipid composition as an adaptation to membrane permeability.
  • thermostable proteins enables thermophilic RO:0002327

    Thermostable proteins retain function during elevated-temperature growth.

    • DOI:10.1128/MMBR.65.1.1-43.2001 resistant to irreversible inactivation at high temperatures Supports thermostability as a high-temperature enzyme feature.
  • energy-transducing enzymes enables thermophilic RO:0002327

    Adapted energy-transducing enzymes support growth at elevated temperature.

    • DOI:10.1016/s0300-9629(97)00003-0 energy transducing enzymes Review cites higher turnover rates and coupling-ion changes in high-temperature adaptation.
  • reverse gyrase introduces positive DNA supercoiling

    Reverse gyrase introduces positive supercoils into thermophile DNA.

    • DOI:10.1264/jsme2.me23087 Takemata 2024: "reverse gyrase introduces positive supercoils" (broadly accepted in thermophile genomics).
  • positive DNA supercoiling limits DNA melting RO:0002212

    Positive DNA supercoiling limits thermal DNA melting, protecting genome integrity.

    • DOI:10.1264/jsme2.me23087 Takemata 2024: "maintain the genome integrity of thermophiles by limiting DNA melting"; mechanism generalized across thermophiles.
  • reverse gyrase mediates genome integrity maintenance

    Reverse gyrase mediates DNA repair and genome-integrity maintenance in thermophiles.

    • DOI:10.1264/jsme2.me23087 Takemata 2024: "maintain the genome integrity of thermophiles by ... mediating DNA repair".
  • group II chaperonin (thermosome) refolds denatured proteins

    The group II chaperonin (thermosome) refolds denatured proteins in an ATP-dependent manner.

    • DOI:10.1128/mbio.03593-22 Baes 2023: "thermosome, which refolds proteins in an ATP-dependent manner".
  • tetraether lipid cyclopentane ring number increases membrane rigidity RO:0002213

    Increased cyclopentane ring number in tetraether lipids increases membrane condensation and rigidity.

    • DOI:10.3389/frbis.2023.1338019 Chong 2024: "cyclopentane ring cyclization ... increase membrane condensation, packing tightness, rigidity".

Provenance

Source
METPO (2025-11-25)
Definition source
DOI:10.1016/s0300-9629(97)00003-0

kg-microbe context

Matched 1 kg-microbe node via direct_metpo.

  • METPO:1000616 [+21.170, -11.999, -10.457, +4.736, …]

512-dim DeepWalkSkipGramEnsmallen embedding from kg-microbe (2026-04-25).

Nearest neighbors in embedding space

Top-8 cosine-similar METPO traits from the 2026-04-25 deepwalk (512-D).

Curation history

  1. · SEEDED_FROM_METPO · seed_from_metpo

    imported from data/raw/metpo.owl (CLASS)

  2. · CURATED_WITH_ORGANISM_EXAMPLE · codex

    Added Geobacillus stearothermophilus organism example with PMID-backed evidence.

  3. · CURATED_WITH_LITERATURE · codex

    Added DOI-backed thermophily causal graph for membrane permeability, lipid adaptation, thermostable proteins, and energy transduction.

  4. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 1 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×1).

  5. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 1 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (METPO:2007401×1).

  6. · RENAME_PREDICATE_LABELS · claude

    Renamed 1 causal-edge predicate label(s) to align with existing groundings: supports → enables ×1.

  7. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 1 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×1).

  8. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 2 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002213×1, RO:0002212×1).

  9. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (PATO:0001305×1).

  10. · REMOVE_REDUNDANT_SYNONYM · claude

    Removed 1 synonym(s) whose text duplicated the label (seeder redundancy; no information lost).

  11. · ENRICH_CAUSAL_GRAPH · claude

    Added 5 evidence-backed generic edges (8 new nodes) from the deep-research report.

  12. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 2 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002212×1, RO:0002213×1).

  13. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (UniProtKB:A0A088E825×1).