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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)DescriptionActionsGraphical viewLength
Active sitei119Charge relay system1
Active sitei161Charge relay system1
Active sitei237Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
PropeptideiPRO_000002688630 – 68By similarityAdd BLAST39
ChainiPRO_000002688769 – 342Glutamyl endopeptidaseAdd BLAST274

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei68 – 69Cleavage; by aureolysinBy similarity2

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ99V45.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV1048.

Structurei

Secondary structure

1342
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi76 – 81Combined sources6
Helixi85 – 87Combined sources3
Beta strandi90 – 97Combined sources8
Beta strandi100 – 110Combined sources11
Beta strandi113 – 116Combined sources4
Helixi118 – 122Combined sources5
Turni123 – 126Combined sources4
Helixi128 – 130Combined sources3
Beta strandi131 – 135Combined sources5
Beta strandi148 – 155Combined sources8
Beta strandi157 – 160Combined sources4
Beta strandi163 – 167Combined sources5
Turni176 – 178Combined sources3
Beta strandi196 – 201Combined sources6
Beta strandi211 – 222Combined sources12
Beta strandi225 – 229Combined sources5
Beta strandi240 – 242Combined sources3
Beta strandi248 – 256Combined sources9
Turni257 – 259Combined sources3
Beta strandi260 – 265Combined sources6
Helixi268 – 277Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ99V45.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati289 – 29113
Repeati292 – 29423
Repeati295 – 29733
Repeati298 – 30043
Repeati301 – 30353
Repeati304 – 30663
Repeati307 – 30973
Repeati310 – 31283
Repeati316 – 31893
Repeati319 – 321103
Repeati322 – 324113
Repeati325 – 327123
Repeati328 – 330133

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni289 – 33013 X 3 AA repeats of P-[DN]-NAdd BLAST42

Sequence similaritiesi

Belongs to the peptidase S1B family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108CHM. Bacteria.
COG3591. LUCA.
KOiK01318.
OMAiNFANDDQ.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QY6X-ray1.90A69-342[»]
2O8LX-ray1.50A69-342[»]
ProteinModelPortaliQ99V45.
SMRiQ99V45.
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.
PhylomeDBiQ99V45.

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...

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: November 2, 2016
This is version 99 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.