Q8NVS9 (SSPP_STAAW) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
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: Staphopain A EC=3.4.22.48 Alternative name(s): Staphylococcal cysteine proteinase A Staphylopain 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: UniProtKB-KW |
| 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]. Strain: MW2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000033 Genomic DNA. Translation: BAB95715.1. |
| RefSeq | NP_646667.1. NC_003923.1. |
3D structure databases | |
| ProteinModelPortal | Q8NVS9. |
| SMR | Q8NVS9. Positions 216-388. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8NVS9. |
Protein family/group databases | |
| MEROPS | C47.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000025747; EBSTAP00000024786; EBSTAG00000025746. |
| GeneID | 1003965. |
| GenomeReviews | Gene locus MW1850 in contig BA000033_GR. |
| KEGG | sam:MW1850. |
| PATRIC | 19570402. VBIStaAur44266_1924. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | NOG43315. |
| GeneTree | EBGT00050000023841. |
| HOGENOM | HBG217891. |
| OMA | YTINVSS. |
| ProtClustDB | CLSK885098. |
Enzyme and pathway databases | |
| BioCyc | SAUR196620:MW1850-MONOMER. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR008750. Peptidase_C47. [Graphical view] |
| KO | K08258. |
| 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 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 |

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