Processes
Conserved receptor/scaffold component that initiates productive Tat-complex assembly around a signal-bearing folded substrate.
A species-neutral bacterial membrane-translocation module for export of folded, twin-arginine-signal-bearing proteins by the TatA, TatB, and TatC machinery. TatC and TatB form the substrate-receptor complex, after which TatA oligomerization supports proton-motive-force-dependent passage across the cytoplasmic membrane. Signal-peptide recognition, receptor assembly, and translocation are modeled as separate substantive roles.
The reusable boundary starts with recognition of a folded Tat substrate and ends with membrane translocation. Cofactor loading and folding of individual substrates are upstream; signal-peptide cleavage and periplasmic destination functions are downstream. Some bacteria encode multiple complete tatABC loci; their physiological division of labor must not be assumed from sequence alone. In P. putida KT2440, PMID:23530902 shows that both complete systems can transport UxpB, but does not establish isolated-subunit activities or broader locus-specific substrate repertoires. The reusable architecture is modeled once here; copy number, operon-specific regulation, and concrete PSEPK satisfiability belong in the species batch rather than in this module.
module.knowledge_gaps[0] · status
(0/1)module.knowledge_gaps[0] · provenance
(0/1)module.knowledge_gaps[1] · status
(0/1)module.knowledge_gaps[1] · provenance
(0/1)✗ none found
No MODULE:bacterial_twin_arginine_translocation deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.
6 complete review(s) · 1 with deep research · 3 missing review · 5 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| Escherichia coli K-12 TatC exemplar P69423 | ✗ | — | — |
| Escherichia coli K-12 TatB exemplar P69425 | ✗ | — | — |
| Escherichia coli K-12 TatA exemplar P69428 | ✗ | — | — |
| tatA-I Q88P12 | ✓ | ✓ | ✗ |
| tatA-II Q88D13 | ✓ | ✓ | ✓ |
| tatB Q88D12 | ✓ | ✓ | ✗ |
| tatB-I Q88P13 | ✓ | ✓ | ✗ |
| tatC-I Q88P14 | ✓ | ✓ | ✗ |
| tatC-II Q88D11 | ✓ | ✓ | ✗ |
TatC provides the multispanning membrane scaffold that recognizes twin-arginine signal peptides together with TatB.
Conserved receptor/scaffold component that initiates productive Tat-complex assembly around a signal-bearing folded substrate.
TatB associates with TatC to organize the substrate receptor and couple substrate recognition to TatA recruitment.
Receptor-associated component required before recruitment of the TatA translocation assembly.
TatA is recruited to the substrate-bound TatBC receptor to form the dynamic, proton-motive-force-dependent translocon.
The assembled TatABC machinery carries out membrane translocation after TatBC-dependent substrate recognition and TatA recruitment.