Reviewed,
UniProtKB/Swiss-Prot Q6GAG4 (SSPA_STAAS)
Last modified
January 19, 2010.
Version 38.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutamyl endopeptidase EC=3.4.21.19 Alternative name(s): Staphylococcal serine proteinase V8 protease V8 proteinase Endoproteinase Glu-C | ||||
| Gene names |
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| Organism | Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282459 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 333 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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. |
| Catalytic activity | Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. |
| Subcellular location | Secreted By similarity. |
| Post-translational modification | Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of sspA By similarity. |
| Miscellaneous | The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through sspA to sspB By similarity. |
| Sequence similarities | Belongs to the peptidase S1B family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Virulence |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Zymogen |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 29 | 29 | Potential | ||||||
| Propeptide | 30 – 68 | 39 | By similarity | PRO_0000026892 | |||||
| Chain | 69 – 333 | 265 | Glutamyl endopeptidase | PRO_0000026893 | |||||
Regions | |||||||||
| Repeat | 289 – 291 | 3 | 1 | ||||||
| Repeat | 292 – 294 | 3 | 2 | ||||||
| Repeat | 295 – 297 | 3 | 3 | ||||||
| Repeat | 298 – 300 | 3 | 4 | ||||||
| Repeat | 301 – 303 | 3 | 5 | ||||||
| Repeat | 304 – 306 | 3 | 6 | ||||||
| Repeat | 307 – 309 | 3 | 7 | ||||||
| Repeat | 310 – 312 | 3 | 8 | ||||||
| Repeat | 313 – 315 | 3 | 9 | ||||||
| Repeat | 316 – 318 | 3 | 10 | ||||||
| Repeat | 319 – 321 | 3 | 11 | ||||||
| Region | 289 – 321 | 33 | 11 X 3 AA repeats of P-[DN]-N | ||||||
Sites | |||||||||
| Active site | 119 | 1 | Charge relay system By similarity | ||||||
| Active site | 161 | 1 | Charge relay system By similarity | ||||||
| Active site | 237 | 1 | Charge relay system By similarity | ||||||
| Site | 68 – 69 | 2 | Cleavage; by aureolysin By similarity | ||||||
Sequences
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References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571857 Genomic DNA. Translation: CAG42759.1. |
| RefSeq | YP_043109.1. |
3D structure databases | |
| SMR | Q6GAG4. Positions 69-284. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6GAG4. |
Genome annotation databases | |
| GeneID | 2862506. |
| GenomeReviews | Gene locus SAS0984 in contig BX571857_GR. |
| KEGG | sas:SAS0984. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3591. |
| HOGENOM | HBG693141. |
| OMA | EDINFAN. |
Enzyme and pathway databases | |
| BioCyc | SAUR282459:SAS0984-MONOMER. |
Family and domain databases | |
| InterPro | IPR000126. Pept_S1B_AS. IPR001254. Peptidase_S1_S6. IPR008256. Peptidase_S1B. IPR008353. Peptidase_S1B_tx. IPR009003. Ser/Cys_Pept_Trypsin-like. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR01774. EXFOLTOXIN. PR00839. V8PROTEASE. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS00672. V8_HIS. 1 hit. PS00673. V8_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SSPA_STAAS | ||||||||
| Accession | Primary (citable) accession number: Q6GAG4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


