Q5HH35 (SSPA_STAAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 59.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutamyl endopeptidase EC=3.4.21.19 Alternative name(s): Endoproteinase Glu-C Staphylococcal serine proteinase V8 protease V8 proteinase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain COL) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93062 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 336 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: UniProtKB-KW |
| 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_0000026884 | |||||
| Chain | 69 – 336 | 268 | Glutamyl endopeptidase | PRO_0000026885 | |||||
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 | 310 – 312 | 3 | 7 | ||||||
| Repeat | 313 – 315 | 3 | 8 | ||||||
| Repeat | 316 – 318 | 3 | 9 | ||||||
| Repeat | 319 – 321 | 3 | 10 | ||||||
| Repeat | 322 – 324 | 3 | 11 | ||||||
| Region | 289 – 324 | 36 | 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] | "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: COL. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000046 Genomic DNA. Translation: AAW36522.1. |
| RefSeq | YP_185922.1. NC_002951.2. |
3D structure databases | |
| ProteinModelPortal | Q5HH35. |
| SMR | Q5HH35. Positions 69-284. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 93062.SACOL1057. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAW36522; AAW36522; SACOL1057. |
| GeneID | 3237584. |
| KEGG | sac:SACOL1057. |
| PATRIC | 19528350. VBIStaAur112458_1028. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3591. |
| HOGENOM | HOG000279966. |
| KO | K01318. |
| OMA | IEDINFA. |
| ProtClustDB | CLSK885099. |
Enzyme and pathway databases | |
| BioCyc | SAUR93062:GCEP-1043-MONOMER. |
Family and domain databases | |
| InterPro | IPR000126. Pept_S1B_AS. IPR001254. Peptidase_S1. IPR008256. Peptidase_S1B. IPR008353. Peptidase_S1B_tx. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| PRINTS | PR01774. EXFOLTOXIN. PR00839. V8PROTEASE. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF50494. Pept_Ser_Cys. 1 hit. |
| PROSITE | PS00672. V8_HIS. 1 hit. PS00673. V8_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SSPA_STAAC | ||||||||
| Accession | Primary (citable) accession number: Q5HH35 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
