Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2G2R8 (SSPP_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Staphopain A

EC=3.4.22.48
Alternative name(s):
Staphylococcal cysteine proteinase A
Staphylopain A
Gene names
Name:sspP
Ordered Locus Names:SAOUHSC_02127
OrganismStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

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

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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_0000247954
Chain215 – 388174Staphopain A
PRO_0000247955

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2G2R8 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 45D76DE341101F0D

FASTA38844,262
        10         20         30         40         50         60 
MKRNFPKLIA LSLIFSLSVT PIANAESNSN IKAKDKKHVQ VNVEDKSVPT DVRNLAQKDY 

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

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

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

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

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

       370        380 
FMTQDAKNNV IPVSNGDHYR WYSSIYGY 

« Hide

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].
Strain: NCTC 8325.
[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

EMBL
GenBank
DDBJ
CP000253 Genomic DNA. Translation: ABD31176.1.
RefSeqYP_500618.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2G2R8.
SMRQ2G2R8. Positions 216-388.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2G2R8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000030247; EBSTAP00000029198; EBSTAG00000030245.
GeneID3921198.
GenomeReviewsGene locus SAOUHSC_02127 in contig CP000253_GR.
KEGGsao:SAOUHSC_02127.
PATRIC19581617. VBIStaAur99865_1930.

Phylogenomic databases

eggNOGNOG43315.
GeneTreeEBGT00050000023841.
HOGENOMHBG217891.
OMAYTINVSS.
ProtClustDBCLSK885098.

Enzyme and pathway databases

BioCycSAUR93061:SAOUHSC_02127-MONOMER.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR008750. Peptidase_C47.
[Graphical view]
KOK08258.
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_STAA8
AccessionPrimary (citable) accession number: Q2G2R8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families