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Protein

Glutamyl endopeptidase

Gene

sspA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Miscellaneous

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

Catalytic activityi

Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei119Charge relay system1
Active sitei161Charge relay system1
Active sitei237Charge relay system1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processVirulence

Protein family/group databases

MEROPSiS01.269

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl endopeptidase (EC:3.4.21.19)
Alternative name(s):
Endoproteinase Glu-C
Staphylococcal serine proteinase
V8 protease
V8 proteinase
Gene namesi
Name:sspA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5115

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
PropeptideiPRO_000002688230 – 681 PublicationAdd BLAST39
ChainiPRO_000002688369 – 336Glutamyl endopeptidaseAdd BLAST268

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei68 – 69Cleavage; by aureolysin2

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiP0C1U8

Interactioni

Protein-protein interaction databases

IntActiP0C1U8, 1 interactor

Chemistry databases

BindingDBiP0C1U8

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0C1U8
SMRiP0C1U8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C1U8

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati289 – 29113
Repeati292 – 29423
Repeati295 – 29733
Repeati298 – 30043
Repeati301 – 30353
Repeati304 – 30663
Repeati310 – 31273
Repeati313 – 31583
Repeati316 – 31893
Repeati319 – 321103
Repeati322 – 324113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni289 – 32411 X 3 AA repeats of P-[DN]-NAdd BLAST36

Sequence similaritiesi

Belongs to the peptidase S1B family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108CHM Bacteria
COG3591 LUCA

Family and domain databases

InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR008256 Peptidase_S1B
IPR008353 Peptidase_S1B_tx
IPR028301 V8_his_AS
IPR000126 V8_ser_AS
PRINTSiPR01774 EXFOLTOXIN
PR00839 V8PROTEASE
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS00672 V8_HIS, 1 hit
PS00673 V8_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C1U8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP
60 70 80 90 100
KIQKGGNLKP LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG
110 120 130 140 150
TFIASGVVVG KDTLLTNKHV VDATHGDPHA LKAFPSAINQ DNYPNGGFTA
160 170 180 190 200
EQITKYSGEG DLAIVKFSPN EQNKHIGEVV KPATMSNNAE TQVNQNITVT
210 220 230 240 250
GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP VFNEKNEVIG
260 270 280 290 300
IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN
310 320 330
PDNPNNPDEP NNPDNPNNPD NPDNGDNNNS DNPDAA
Length:336
Mass (Da):36,326
Last modified:September 5, 2006 - v1
Checksum:i8B138D0C7996AA3E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti109Missing AA sequence (PubMed:96922).Curated1
Sequence conflicti125Missing AA sequence (PubMed:96922).Curated1
Sequence conflicti145N → D AA sequence (PubMed:96922).Curated1
Sequence conflicti193V → T AA sequence (PubMed:96922).Curated1
Sequence conflicti229D → N AA sequence (PubMed:96922).Curated1
Sequence conflicti259 – 261EFN → QFD AA sequence (PubMed:96922).Curated3
Sequence conflicti268 – 270ENV → NEVN AA sequence (PubMed:96922).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00356 Genomic DNA Translation: CAA68434.1
PIRiA26812 PRSASK
RefSeqiWP_000676548.1, NZ_UHCV01000002.1

Similar proteinsi

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00356 Genomic DNA Translation: CAA68434.1
PIRiA26812 PRSASK
RefSeqiWP_000676548.1, NZ_UHCV01000002.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WCZX-ray2.00A69-336[»]
ProteinModelPortaliP0C1U8
SMRiP0C1U8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C1U8, 1 interactor

Chemistry databases

BindingDBiP0C1U8
ChEMBLiCHEMBL5115

Protein family/group databases

MEROPSiS01.269

Proteomic databases

PRIDEiP0C1U8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108CHM Bacteria
COG3591 LUCA

Miscellaneous databases

EvolutionaryTraceiP0C1U8
PROiPR:P0C1U8

Family and domain databases

InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR008256 Peptidase_S1B
IPR008353 Peptidase_S1B_tx
IPR028301 V8_his_AS
IPR000126 V8_ser_AS
PRINTSiPR01774 EXFOLTOXIN
PR00839 V8PROTEASE
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS00672 V8_HIS, 1 hit
PS00673 V8_SER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSSPA_STAAU
AccessioniPrimary (citable) accession number: P0C1U8
Secondary accession number(s): P04188
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: November 7, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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