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Q2FZL2 (SSPA_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 53. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl endopeptidase

EC=3.4.21.19
Alternative name(s):
Endoproteinase Glu-C
Staphylococcal serine proteinase
V8 protease
V8 proteinase
Gene names
Name:sspA
Ordered Locus Names:SAOUHSC_00988
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. Ref.1 Ref.3 Ref.5 Ref.7

Catalytic activity

Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.

Subcellular location

Secreted By similarity.

Induction

Expression occurs in a growth-phase-dependent manner with optimal expression at post-exponential phase. Environmental conditions such as degree of aeration and salt concentration are also important in control of transcription and processing of SspA. Up-regulated by Agr (accessory gene regulator) and repressed by sigmaB factor and SarA. Ref.3 Ref.4 Ref.6

Post-translational modification

Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA.

Miscellaneous

The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through SspA to SspB.

Sequence similarities

Belongs to the peptidase S1B family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionHydrolase
Protease
Serine 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_functionserine-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 – 2929 Potential
Propeptide30 – 6839
PRO_0000249327
Chain69 – 336268Glutamyl endopeptidase
PRO_0000249328

Regions

Repeat289 – 29131
Repeat292 – 29432
Repeat295 – 29733
Repeat298 – 30034
Repeat301 – 30335
Repeat304 – 30636
Repeat310 – 31237
Repeat313 – 31538
Repeat316 – 31839
Repeat319 – 321310
Repeat322 – 324311
Region289 – 3243611 X 3 AA repeats of P-[DN]-N

Sites

Active site1191Charge relay system By similarity
Active site1611Charge relay system By similarity
Active site2371Charge relay system By similarity
Site68 – 692Cleavage; by aureolysin

Sequences

Sequence LengthMass (Da)Tools
Q2FZL2 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 8B138D0C7996AA3E

FASTA33636,326
        10         20         30         40         50         60 
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP KIQKGGNLKP 

        70         80         90        100        110        120 
LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV 

       130        140        150        160        170        180 
VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV 

       190        200        210        220        230        240 
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP 

       250        260        270        280        290        300 
VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN 

       310        320        330 
PDNPNNPDEP NNPDNPNNPD NPDNGDNNNS DNPDAA 

« Hide

References

« Hide 'large scale' references
[1]"Description of Staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease."
Rice K., Peralta R., Bast D., de Azavedo J., McGavin M.J.
Infect. Immun. 69:159-169(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"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.
[3]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-76, FUNCTION, INDUCTION.
[4]"Interactive regulatory pathways control virulence determinant production and stability in response to environmental conditions in Staphylococcus aureus."
Lindsay J.A., Foster S.J.
Mol. Gen. Genet. 262:323-331(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION.
[5]"Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases."
Karlsson A., Saravia-Otten P., Tegmark K., Morfeldt E., Arvidson S.
Infect. Immun. 69:4742-4748(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Variation in extracellular protease production among clinical isolates of Staphylococcus aureus due to different levels of expression of the protease repressor sarA."
Karlsson A., Arvidson S.
Infect. Immun. 70:4239-4246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Identification of a novel maturation mechanism and restricted substrate specificity for the sspB cysteine protease of Staphylococcus aureus."
Massimi I., Park E., Rice K., Mueller-Esterl W., Sauder D., McGavin M.J.
J. Biol. Chem. 277:41770-41777(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF309515 Genomic DNA. Translation: AAG45843.1.
CP000253 Genomic DNA. Translation: ABD30113.1.
RefSeqYP_499541.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2FZL2.
SMRQ2FZL2. Positions 69-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00988.

Proteomic databases

PRIDEQ2FZL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30113; ABD30113; SAOUHSC_00988.
GeneID3920389.
KEGGsao:SAOUHSC_00988.
PATRIC19579499. VBIStaAur99865_0908.

Phylogenomic databases

eggNOGCOG3591.
HOGENOMHOG000279966.
KOK01318.
OMAIEDINFA.
OrthoDBEOG6423F5.
ProtClustDBCLSK885099.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-954-MONOMER.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR009003. Trypsin-like_Pept_dom.
IPR028301. V8_his_AS.
IPR000126. V8_ser_AS.
[Graphical view]
PRINTSPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ2FZL2.

Entry information

Entry nameSSPA_STAA8
AccessionPrimary (citable) accession number: Q2FZL2
Secondary accession number(s): P04188
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 21, 2006
Last modified: November 13, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries