A0A5C9T5J2 · A0A5C9T5J2_VIBCL
- 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 | 128 | ||||
Active site | 146 | ||||
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 > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionA0A5C9T5J2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 15-33 | Helical | |||
Transmembrane | 45-66 | Helical | |||
Transmembrane | 72-92 | Helical | |||
Transmembrane | 104-125 | Helical | |||
Transmembrane | 137-158 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length171
- Mass (Da)19,418
- Last updated2021-09-29 v1
- ChecksumB550740E98B5E2B0
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VSGZ01000002 EMBL· GenBank· DDBJ | TXY94583.1 EMBL· GenBank· DDBJ | Genomic DNA |