Q99V45 · SSPA_STAAM
- ProteinGlutamyl endopeptidase
- GenesspA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids342 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).
Miscellaneous
The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through SspA to SspB.
Catalytic activity
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 68-69 | Cleavage; by aureolysin | ||||
Sequence: NV | ||||||
Active site | 119 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 161 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 237 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutamyl endopeptidase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionQ99V45
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MKGKFLKVSSLFVATLTTATLVSSPAANA | ||||||
Propeptide | PRO_0000026886 | 30-68 | ||||
Sequence: LSSKAMDNHPQQTQSSKQQTPKIKKGGNLKPLEQREHAN | ||||||
Chain | PRO_0000026887 | 69-342 | Glutamyl endopeptidase | |||
Sequence: VILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA |
Post-translational modification
Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA (By similarity).
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 33-52 | Polar residues | ||||
Sequence: KAMDNHPQQTQSSKQQTPKI | ||||||
Region | 33-63 | Disordered | ||||
Sequence: KAMDNHPQQTQSSKQQTPKIKKGGNLKPLEQ | ||||||
Region | 283-342 | Disordered | ||||
Sequence: FANDDQPNNPDNPDNPNNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA | ||||||
Repeat | 289-291 | 1 | ||||
Sequence: PNN | ||||||
Region | 289-330 | 13 X 3 AA repeats of P-[DN]-N | ||||
Sequence: PNNPDNPDNPNNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDN | ||||||
Repeat | 292-294 | 2 | ||||
Sequence: PDN | ||||||
Compositional bias | 294-323 | Pro residues | ||||
Sequence: NPDNPNNPDNPNNPDNPNNPDEPNNPDNPN | ||||||
Repeat | 295-297 | 3 | ||||
Sequence: PDN | ||||||
Repeat | 298-300 | 4 | ||||
Sequence: PNN | ||||||
Repeat | 301-303 | 5 | ||||
Sequence: PDN | ||||||
Repeat | 304-306 | 6 | ||||
Sequence: PNN | ||||||
Repeat | 307-309 | 7 | ||||
Sequence: PDN | ||||||
Repeat | 310-312 | 8 | ||||
Sequence: PNN | ||||||
Repeat | 316-318 | 9 | ||||
Sequence: PNN | ||||||
Repeat | 319-321 | 10 | ||||
Sequence: PDN | ||||||
Repeat | 322-324 | 11 | ||||
Sequence: PNN | ||||||
Compositional bias | 324-342 | Polar residues | ||||
Sequence: NPDNPDNGDNNNSDNPDAA | ||||||
Repeat | 325-327 | 12 | ||||
Sequence: PDN | ||||||
Repeat | 328-330 | 13 | ||||
Sequence: PDN |
Sequence similarities
Belongs to the peptidase S1B family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length342
- Mass (Da)36,977
- Last updated2001-06-01 v1
- Checksum5AEF42DCE01C4B24
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 33-52 | Polar residues | ||||
Sequence: KAMDNHPQQTQSSKQQTPKI | ||||||
Compositional bias | 294-323 | Pro residues | ||||
Sequence: NPDNPNNPDNPNNPDNPNNPDEPNNPDNPN | ||||||
Compositional bias | 324-342 | Polar residues | ||||
Sequence: NPDNPDNGDNNNSDNPDAA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000017 EMBL· GenBank· DDBJ | BAB57210.1 EMBL· GenBank· DDBJ | Genomic DNA |