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Protein

Glutamyl endopeptidase

Gene

sspA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei119 – 1191Charge relay system
Active sitei161 – 1611Charge relay system
Active sitei237 – 2371Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

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

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5115.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Propeptidei30 – 68391 PublicationPRO_0000026882Add
BLAST
Chaini69 – 336268Glutamyl endopeptidasePRO_0000026883Add
BLAST

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei68 – 692Cleavage; by aureolysin

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiP0C1U8.

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL1057.

Chemistry

BindingDBiP0C1U8.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi75 – 806Combined sources
Helixi85 – 873Combined sources
Beta strandi90 – 967Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi110 – 1167Combined sources
Helixi118 – 1214Combined sources
Helixi122 – 1243Combined sources
Helixi128 – 1303Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi163 – 1675Combined sources
Helixi176 – 1794Combined sources
Beta strandi196 – 2016Combined sources
Beta strandi211 – 22212Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi248 – 2569Combined sources
Turni257 – 2593Combined sources
Beta strandi260 – 2656Combined sources
Helixi268 – 27710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WCZX-ray2.00A69-336[»]
ProteinModelPortaliP0C1U8.
SMRiP0C1U8. Positions 69-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C1U8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati289 – 29131
Repeati292 – 29432
Repeati295 – 29733
Repeati298 – 30034
Repeati301 – 30335
Repeati304 – 30636
Repeati310 – 31237
Repeati313 – 31538
Repeati316 – 31839
Repeati319 – 321310
Repeati322 – 324311

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni289 – 3243611 X 3 AA repeats of P-[DN]-NAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1B family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108CHM. Bacteria.
COG3591. LUCA.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR028301. V8_his_AS.
IPR000126. V8_ser_AS.
[Graphical view]
PRINTSiPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091Missing AA sequence (PubMed:96922).Curated
Sequence conflicti125 – 1251Missing AA sequence (PubMed:96922).Curated
Sequence conflicti145 – 1451N → D AA sequence (PubMed:96922).Curated
Sequence conflicti193 – 1931V → T AA sequence (PubMed:96922).Curated
Sequence conflicti229 – 2291D → N AA sequence (PubMed:96922).Curated
Sequence conflicti259 – 2613EFN → QFD AA sequence (PubMed:96922).Curated
Sequence conflicti268 – 2703ENV → NEVN AA sequence (PubMed:96922).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00356 Genomic DNA. Translation: CAA68434.1.
PIRiA26812. PRSASK.
RefSeqiWP_000676548.1. NZ_LOSC01000004.1.

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_LOSC01000004.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WCZX-ray2.00A69-336[»]
ProteinModelPortaliP0C1U8.
SMRiP0C1U8. Positions 69-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1057.

Chemistry

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.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR028301. V8_his_AS.
IPR000126. V8_ser_AS.
[Graphical view]
PRINTSiPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8."
    Carmona C., Gray G.L.
    Nucleic Acids Res. 15:6757-6757(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 27733 / V8.
  2. "The primary structure of staphylococcal protease."
    Drapeau G.R.
    Can. J. Biochem. 56:534-544(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 69-280.
    Strain: ATCC 27733 / V8.
  3. "Purification and properties of an extracellular protease of Staphylococcus aureus."
    Drapeau G.R., Boily Y., Houmard J.
    J. Biol. Chem. 247:6720-6726(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Strain: ATCC 27733 / V8.
  4. "Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus."
    Prokesova L., Potuznikova B., Potempa J., Zikan J., Radl J., Hachova L., Baran K., Porwit-Bobr Z., John C.
    Immunol. Lett. 31:259-265(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: ATCC 27733 / V8.
  5. "Crystal structure of an alkaline form of V8 protease from Staphylococcus aureus."
    Yamada K., Ohta M., Hasegawa T., Torii K., Murakami M., Kouyama K.
    Submitted (JUN-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 69-336.
    Strain: ATCC 27733 / V8.

Entry informationi

Entry nameiSSPA_STAAU
AccessioniPrimary (citable) accession number: P0C1U8
Secondary accession number(s): P04188
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: May 11, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.