Reviewed,
UniProtKB/Swiss-Prot Q8NVS9 (SSPP_STAAW)
Last modified
June 16, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Staphopain A EC=3.4.22.48 Alternative name(s): Staphylopain A Staphylococcal cysteine proteinase A | ||||||
| Gene names |
| ||||||
| Organism | Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 196620 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 388 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 | Cysteine protease able to degrade elastin By similarity. |
| Catalytic activity | Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate. |
| Enzyme regulation | Prematurely activated/folded staphopain A is inhibited by staphostatin A (scpB), which is probably required to protect staphylococcal cytoplasmic proteins from degradation by scpA By similarity. |
| Subunit structure | In the cytoplasm, prematurely activated/folded scpA forms a stable non-covalent complex with scpB By similarity. |
| Subcellular location | Secreted By similarity. |
| Post-translational modification | Cleavage leads to the activation of scpA probably by an auto-catalytic manner By similarity. |
| Miscellaneous | The catalytic maturation of scpA appears to reside outside the cascade of activation started by the metalloprotease aureolysin (aur) By similarity. |
| Sequence similarities | Belongs to the peptidase C47 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Virulence |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Thiol 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 | cysteine-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 – 25 | 25 | Potential | ||||||
| Propeptide | 26 – 214 | 189 | By similarity | PRO_0000026557 | |||||
| Chain | 215 – 388 | 174 | Staphopain A | PRO_0000026558 | |||||
Sites | |||||||||
| Active site | 238 | 1 | By similarity | ||||||
| Active site | 334 | 1 | By similarity | ||||||
| Active site | 355 | 1 | By similarity | ||||||
| Site | 214 – 215 | 2 | Cleavage By similarity | ||||||
Sequences
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References
| [1] | "Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BA000033 Genomic DNA. Translation: BAB95715.1. | |
| RefSeq | NP_646667.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CV8 based on UniProtKB P81297. |
| SMR | Q8NVS9. Positions 216-388. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C47.001. |
Genome annotation databases | |
| GeneID | 1003965. |
| GenomeReviews | Gene locus MW1850 in contig BA000033_GR. |
| KEGG | sam:MW1850. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8NVS9. |
| OMA | Q8NVS9. YTINVSS. |
Enzyme and pathway databases | |
| BioCyc | SAUR196620:MW1850-MON. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR008750. Peptidase_C47. [Graphical view] |
| Pfam | PF05543. Peptidase_C47. 1 hit. [Graphical view] |
| PROSITE | PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. False negative. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SSPP_STAAW | ||||||||
| Accession | Primary (citable) accession number: Q8NVS9 | ||||||||
| 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


