A0A2D2MBF3 · A0A2D2MBF3_9PSED
- ProteinLipoprotein signal peptidase
- GenelspA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids171 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic activity
Pathway
Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 126 | |||||
Sequence: D | ||||||
Active site | 145 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | aspartic-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoprotein signal peptidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A2D2MBF3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 73-90 | Helical | ||||
Sequence: WLFALIALVVSAVLVVWL | ||||||
Transmembrane | 97-116 | Helical | ||||
Sequence: DTWLAVALALVLGGALGNLY | ||||||
Transmembrane | 136-157 | Helical | ||||
Sequence: WYFPAFNLADSAITVGAVMLAL |
Keywords
- Cellular component
Structure
Sequence
- Sequence statusComplete
- Length171
- Mass (Da)19,194
- Last updated2018-01-31 v1
- Checksum683B187B0D2D0D2C
Keywords
- Technical term