DB code: D00851

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.19
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq MEROPS
Q99V45 Glutamyl endopeptidase
V8 protease
V8 proteinase
EC 3.4.21.19
Endoproteinase Glu-C
Staphylococcal serine proteinase
NP_371572.1 (Protein)
NC_002758.2 (DNA/RNA sequence)
P0C1U8 Glutamyl endopeptidase
EC 3.4.21.19
Endoproteinase Glu-C
Staphylococcal serine proteinase
V8 protease
V8 proteinase
S01.269 (Serine)

KEGG enzyme name
Glutamyl endopeptidase
V8 proteinase
Endoproteinase Glu-C
Staphylococcal serine proteinase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q99V45 SSPA_STAAM Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. Secreted (By similarity).
P0C1U8 SSPA_STAAU Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00001 C00017 I00087 I00085 I00086
E.C.
Compound Protein H2O Protein Peptidyl-Ser-tetrahedral-intermediate (with previous peptide) Acyl-enzyme(Peptidyl-Ser-acyl group) Peptidyl-Ser-tetrahedral-intermediate
Type peptide/protein H2O peptide/protein
ChEBI 15377
PubChem 22247451
962
1wczA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qy6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2o8lA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1wczA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qy6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2o8lA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [4] & Swiss-prot;P0C1U8, Q99V45

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1wczA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 169 GLY 167;SER 169
1qy6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 169 GLY 167;SER 169
2o8lA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 169 GLY 167;SER 169
1wczA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 51;ASP 93
1qy6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 51;ASP 93
2o8lA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 51;ASP 93

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Figure 5, p.4505-4508

References
[1]
Resource
Comments
Medline ID
PubMed ID 4509307
Journal Proc Natl Acad Sci U S A
Year 1972
Volume 69
Pages 3506-9
Authors Houmard J, Drapeau GR
Title Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 136253
Journal Biochem Biophys Res Commun
Year 1976
Volume 72
Pages 411-7
Authors Austen BM, Smith EL
Title Action of staphylococcal proteinase on peptides of varying chain length and composition.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 12475199
Journal Chem Rev
Year 2002
Volume 102
Pages 4501-24
Authors Hedstrom L
Title Serine protease mechanism and specificity.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 69-342.
Medline ID
PubMed ID 14747701
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 256-9
Authors Prasad L, Leduc Y, Hayakawa K, Delbaere LT
Title The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus.
Related PDB 1qy6 2o8l
Related UniProtKB Q99V45
[5]
Resource
Comments
Medline ID
PubMed ID 17878159
Journal J Biol Chem
Year 2007
Volume 282
Pages 34129-38
Authors Nickerson NN, Prasad L, Jacob L, Delbaere LT, McGavin MJ
Title Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to peptidase family-S1B.
Since this enzyme has got the same catalytic site as trypsin, it must catalyze the trypsin-like reaction.

Created Updated
2011-02-24 2012-07-31