Protein · Aquifex aeolicus VF5
pilD · Type 4 prepilin peptidase
Unspecified254 amino acidsaq_1601 · O67535
How it works
Prepilin peptidase (PilD). It trims the leader off pilin-like proteins in the inner membrane before they are assembled.
- Overall
- UniProt gives no function statement yet.
- What it does
- No catalysed reaction annotated.
- Structure
- AlphaFold DB
- Components
- Prepilin peptidase A24 N-terminal residues 12–94
- Prepilin type IV endopeptidase peptidase residues 106–214
- 5 membrane-crossing segments
- Amino acids
- 254 · 28.6 kDa
- Reaction core
- No active-site residues annotated.
- Metal or cluster
- None annotated.
- Where it works
- Not yet placed in a pathway in Conserved, but we cannot say what they do
- How sure we are
- Unspecified We know only that related organisms keep it. Neither the step nor the system can be named.
The short description is the atlas’s own; the details below it are from UniProt and the atlas inventory.
How it is built and controlled
- Made from its gene pilD (locus aq_1601) by transcription and translation.
- Location: Cell inner membrane.
- As a membrane protein it must be inserted into the membrane after or during synthesis.
This protein is not on the control-layer lists for information, signaling, regulation, signals inside machines or assembly.
Which regulator controls its gene is not established for Aquifex, which has no genetic system for testing it. See the control layer for conserved, but we cannot say what they do.
Origins
The history of how this protein was discovered and the origins analysis are written in phase 3. Until then, see the origins for conserved, but we cannot say what they do.