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Q99V45 (SSPA_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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:SAV1048
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length342 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 By similarity.

Catalytic activity

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

Subcellular location

Secreted By similarity.

Post-translational modification

Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of sspA By similarity.

Miscellaneous

The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through sspA to sspB By similarity.

Sequence similarities

Belongs to the peptidase S1B family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMZymogen
   Technical term3D-structure
Complete 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 By similarity
PRO_0000026886
Chain69 – 342274Glutamyl endopeptidase
PRO_0000026887

Regions

Repeat289 – 29131
Repeat292 – 29432
Repeat295 – 29733
Repeat298 – 30034
Repeat301 – 30335
Repeat304 – 30636
Repeat307 – 30937
Repeat310 – 31238
Repeat316 – 31839
Repeat319 – 321310
Repeat322 – 324311
Repeat325 – 327312
Repeat328 – 330313
Region289 – 3304213 X 3 AA repeats of P-[DN]-N

Sites

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

Secondary structure

1 ....................................... 342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99V45 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5AEF42DCE01C4B24

FASTA34236,977
        10         20         30         40         50         60 
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP KIKKGGNLKP 

        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        340 
PDNPNNPDNP NNPDEPNNPD NPNNPDNPDN GDNNNSDNPD AA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000017 Genomic DNA. Translation: BAB57210.1.
RefSeqNP_371572.1. NC_002758.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QY6X-ray1.90A69-342[»]
2O8LX-ray1.50A69-342[»]
ProteinModelPortalQ99V45.
SMRQ99V45. Positions 69-284.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99V45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000006350; EBSTAP00000006168; EBSTAG00000006349.
GeneID1121025.
GenomeReviewsGene locus SAV1048 in contig BA000017_GR.
KEGGsav:SAV1048.
PATRIC19562793. VBIStaAur52173_1075.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3591.
GeneTreeEBGT00050000023734.
HOGENOMHBG693141.
OMAEDINFAN.
ProtClustDBCLSK885099.

Enzyme and pathway databases

BioCycSAUR158878:SAV1048-MONOMER.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR000126. Pept_S1B_AS.
IPR001254. Peptidase_S1_S6.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
[Graphical view]
KOK01318.
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSSPA_STAAM
AccessionPrimary (citable) accession number: Q99V45
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 67 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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