Q2FZL2 · SSPA_STAA8
- ProteinGlutamyl endopeptidase
- GenesspA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
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 accessionQ2FZL2
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for signal, propeptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MKGKFLKVSSLFVATLTTATLVSSPAANA | ||||||
Propeptide | PRO_0000249327 | 30-68 | ||||
Sequence: LSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHAN | ||||||
Chain | PRO_0000249328 | 69-336 | Glutamyl endopeptidase | |||
Sequence: VILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA |
Post-translational modification
Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA.
Keywords
- PTM
Proteomic databases
Expression
Induction
Expression occurs in a growth-phase-dependent manner with optimal expression at post-exponential phase. Environmental conditions such as degree of aeration and salt concentration are also important in control of transcription and processing of SspA. Up-regulated by Agr (accessory gene regulator) and repressed by sigmaB factor and SarA.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 34-54 | Polar residues | ||||
Sequence: AMDNHPQQTQSSKQQTPKIQK | ||||||
Region | 34-61 | Disordered | ||||
Sequence: AMDNHPQQTQSSKQQTPKIQKGGNLKPL | ||||||
Region | 283-336 | Disordered | ||||
Sequence: FANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA | ||||||
Repeat | 289-291 | 1 | ||||
Sequence: PNN | ||||||
Region | 289-324 | 11 X 3 AA repeats of P-[DN]-N | ||||
Sequence: PNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDN | ||||||
Repeat | 292-294 | 2 | ||||
Sequence: PDN | ||||||
Compositional bias | 294-317 | Pro residues | ||||
Sequence: NPDNPNNPDNPNNPDEPNNPDNPN | ||||||
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 | 310-312 | 7 | ||||
Sequence: PNN | ||||||
Repeat | 313-315 | 8 | ||||
Sequence: PDN | ||||||
Repeat | 316-318 | 9 | ||||
Sequence: PNN | ||||||
Compositional bias | 318-336 | Polar residues | ||||
Sequence: NPDNPDNGDNNNSDNPDAA | ||||||
Repeat | 319-321 | 10 | ||||
Sequence: PDN | ||||||
Repeat | 322-324 | 11 | ||||
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.
- Length336
- Mass (Da)36,326
- Last updated2006-03-21 v1
- Checksum8B138D0C7996AA3E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 34-54 | Polar residues | ||||
Sequence: AMDNHPQQTQSSKQQTPKIQK | ||||||
Compositional bias | 294-317 | Pro residues | ||||
Sequence: NPDNPNNPDNPNNPDEPNNPDNPN | ||||||
Compositional bias | 318-336 | Polar residues | ||||
Sequence: NPDNPDNGDNNNSDNPDAA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF309515 EMBL· GenBank· DDBJ | AAG45843.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000253 EMBL· GenBank· DDBJ | ABD30113.1 EMBL· GenBank· DDBJ | Genomic DNA |