P65825 (SSPP_STAAM) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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 Mu50 / ATCC 700699) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 158878 [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_0000026549 | |||||
| Chain | 215 – 388 | 174 | Staphopain A | PRO_0000026550 | |||||
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] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu50 / ATCC 700699. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000017 Genomic DNA. Translation: BAB58071.1. |
| RefSeq | NP_372433.1. NC_002758.2. |
3D structure databases | |
| ProteinModelPortal | P65825. |
| SMR | P65825. Positions 216-388. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P65825. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000005963; EBSTAP00000005781; EBSTAG00000005962. |
| GeneID | 1121922. |
| GenomeReviews | Gene locus SAV1909 in contig BA000017_GR. |
| KEGG | sav:SAV1909. |
| PATRIC | 19564672. VBIStaAur52173_1976. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | NOG43315. |
| GeneTree | EBGT00050000023841. |
| HOGENOM | HBG217891. |
| OMA | YTINVSS. |
| ProtClustDB | CLSK885098. |
Enzyme and pathway databases | |
| BioCyc | SAUR158878:SAV1909-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_STAAM | ||||||||
| Accession | Primary (citable) accession number: P65825 Secondary accession number(s): Q99SX8 | ||||||||
| 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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