Reviewed,
UniProtKB/Swiss-Prot Q2G2R8 (SSPP_STAA8)
Last modified
June 16, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 NCTC 8325) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93061 [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 | Evidence at protein level. |
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. |
| Induction | Expression occurs in a growth phase-dependent manner with optimal expression at post-exponential phase. Up-regulated by agr (accessory gene regulator) and repressed by sarA (staphylococcal accessory regulator) and sigmaB factor. Ref.2 |
| 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 Direct protein sequencing |
| 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_0000247954 | |||||
| Chain | 215 – 388 | 174 | Staphopain A | PRO_0000247955 | |||||
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
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "The role and regulation of the extracellular proteases of Staphylococcus aureus." Shaw L., Golonka E., Potempa J., Foster S.J. Microbiology 150:217-228(2004) [PubMed: 14702415] [Abstract] Cited for: PROTEIN SEQUENCE OF 215-222, INDUCTION. |
Cross-references
Sequence databases | |
|---|---|
| CP000253 Genomic DNA. Translation: ABD31176.1. | |
| RefSeq | YP_500618.1. |
3D structure databases | |
| SMR | Q2G2R8. Positions 216-388. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3921198. |
| GenomeReviews | Gene locus SAOUHSC_02127 in contig CP000253_GR. |
| KEGG | sao:SAOUHSC_02127. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q2G2R8. |
| OMA | Q2G2R8. YTINVSS. |
Enzyme and pathway databases | |
| BioCyc | SAUR93061:SAOUHSC_02127-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_STAA8 | ||||||||
| Accession | Primary (citable) accession number: Q2G2R8 | ||||||||
| Entry history |
| ||||||||
| 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


