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Reviewed, UniProtKB/Swiss-Prot Q8NVS9 (SSPP_STAAW)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Staphopain A
    EC=3.4.22.48
Alternative name(s):
    Staphylopain A
    Staphylococcal cysteine proteinase A
Gene names
Name: sspP
Synonyms: scpA
Ordered Locus Names: MW1850
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 214189 By similarity
PRO_0000026557
Chain215 – 388174Staphopain A
PRO_0000026558

Sites

Active site2381 By similarity
Active site3341 By similarity
Active site3551 By similarity
Site214 – 2152Cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NVS9-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0D502FD9F50933F7

FASTA38844,142
        10         20         30         40         50         60 
MKRNFPKLIA LSLILSLSVT PIANAESNSN IKAKDKKHVQ VNVEDKSIPT EVRNLAQKDY 

        70         80         90        100        110        120 
LSYVTSLDKI YNKEKASYTL GEPFKIYKFN KKSDGNYYFP VLNTEGNIDY IVTISPKVTK 

       130        140        150        160        170        180 
YSSSSSKYTI NVSPFLSKVL NQYKDQQITI LTNSKGYYVV TQNHKAKLVL KTPRLEDKKL 

       190        200        210        220        230        240 
KKTESIPTGN NVTQLKQKAS VTMPTSQFKS NNYTYNEQYV NKLENFKIRE TQGNNGWCAG 

       250        260        270        280        290        300 
YTMSALLNAT YNTNKYHAEA VMRFLHPNLQ GQRFQFTGLT PREMIYFGQT QGRSPQLLNR 

       310        320        330        340        350        360 
MTTYNEVDNL TKNNKGIAVL GSRVESRNGM HAGHAMAVVG NAKLDNGQEV IIIWNPWDNG 

       370        380 
FMTQDAKNNV IPVSNGDHYQ WYSSIYGY 

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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.
RefSeqNP_646667.1.

3D structure databases

HSSPHSSP built from PDB template 1CV8 based on UniProtKB P81297.
SMRQ8NVS9. Positions 216-388.
ModBaseSearch...

Protein family/group databases

MEROPSC47.001.

Genome annotation databases

GeneID1003965.
GenomeReviewsGene locus MW1850 in contig BA000033_GR.
KEGGsam:MW1850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8NVS9.
OMAQ8NVS9. YTINVSS.

Enzyme and pathway databases

BioCycSAUR196620:MW1850-MON.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR008750. Peptidase_C47.
[Graphical view]
PfamPF05543. Peptidase_C47. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. False negative.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSSPP_STAAW
AccessionPrimary (citable) accession number: Q8NVS9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents