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Protein

Glutamyl endopeptidase

Gene

sspA

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1068-MONOMER.

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
Ordered Locus Names:SAV1048
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Propeptidei30 – 6839By similarityPRO_0000026886Add
BLAST
Chaini69 – 342274Glutamyl endopeptidasePRO_0000026887Add
BLAST

Post-translational modificationi

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

Sites

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

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ99V45.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV1048.

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi76 – 816Combined sources
Helixi85 – 873Combined sources
Beta strandi90 – 978Combined sources
Beta strandi100 – 11011Combined sources
Beta strandi113 – 1164Combined sources
Helixi118 – 1225Combined sources
Turni123 – 1264Combined sources
Helixi128 – 1303Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi163 – 1675Combined sources
Turni176 – 1783Combined sources
Beta strandi196 – 2016Combined sources
Beta strandi211 – 22212Combined sources
Beta strandi225 – 2295Combined 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
1QY6X-ray1.90A69-342[»]
2O8LX-ray1.50A69-342[»]
ProteinModelPortaliQ99V45.
SMRiQ99V45. Positions 69-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99V45.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati289 – 29131
Repeati292 – 29432
Repeati295 – 29733
Repeati298 – 30034
Repeati301 – 30335
Repeati304 – 30636
Repeati307 – 30937
Repeati310 – 31238
Repeati316 – 31839
Repeati319 – 321310
Repeati322 – 324311
Repeati325 – 327312
Repeati328 – 330313

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni289 – 3304213 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.
KOiK01318.
OMAiNFANDDQ.
OrthoDBiEOG6423F5.
PhylomeDBiQ99V45.

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.

Q99V45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP
60 70 80 90 100
KIKKGGNLKP 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
310 320 330 340
PDNPNNPDNP NNPDEPNNPD NPNNPDNPDN GDNNNSDNPD AA
Length:342
Mass (Da):36,977
Last modified:June 1, 2001 - v1
Checksum:i5AEF42DCE01C4B24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57210.1.
RefSeqiWP_000676539.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57210; BAB57210; SAV1048.
KEGGisav:SAV1048.
PATRICi19562793. VBIStaAur52173_1075.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57210.1.
RefSeqiWP_000676539.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QY6X-ray1.90A69-342[»]
2O8LX-ray1.50A69-342[»]
ProteinModelPortaliQ99V45.
SMRiQ99V45. Positions 69-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1048.

Proteomic databases

PaxDbiQ99V45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57210; BAB57210; SAV1048.
KEGGisav:SAV1048.
PATRICi19562793. VBIStaAur52173_1075.

Phylogenomic databases

eggNOGiENOG4108CHM. Bacteria.
COG3591. LUCA.
KOiK01318.
OMAiNFANDDQ.
OrthoDBiEOG6423F5.
PhylomeDBiQ99V45.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1068-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ99V45.
PROiQ99V45.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.
  2. "The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus."
    Prasad L., Leduc Y., Hayakawa K., Delbaere L.T.J.
    Acta Crystallogr. D 60:256-259(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 69-342.

Entry informationi

Entry nameiSSPA_STAAM
AccessioniPrimary (citable) accession number: Q99V45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 96 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.By similarity

Keywords - Technical termi

3D-structure, Complete proteome

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.