EzCatDB: D00851
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DB codeD00851
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.19

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,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

Enzyme Name
UniProtKBKEGG

P0C1U8Q99V45
Protein nameGlutamyl endopeptidaseGlutamyl endopeptidaseGlutamyl endopeptidase
V8 proteinase
Endoproteinase Glu-C
Staphylococcal serine proteinase
SynonymsEC 3.4.21.19
Endoproteinase Glu-C
Staphylococcal serine proteinase
V8 protease
V8 proteinase
EC 3.4.21.19
Endoproteinase Glu-C
Staphylococcal serine proteinase
V8 protease
V8 proteinase
RefSeq
NP_371572.1 (Protein)
NC_002758.2 (DNA/RNA sequence)
MEROPSS01.269 (Serine)



UniProtKB:Accession NumberP0C1U8Q99V45
Entry nameSSPA_STAAUSSPA_STAAM
ActivityPreferential cleavage: Glu-|-Xaa, Asp-|-Xaa.Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
Subunit

Subcellular locationSecreted.Secreted (By similarity).
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00001C00017I00087I00085I00086
CompoundProteinH2OProteinPeptidyl-Ser-tetrahedral-intermediate (with previous peptide)Acyl-enzyme(Peptidyl-Ser-acyl group)Peptidyl-Ser-tetrahedral-intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem
962
22247451




              
1wczA01Unbound UnboundUnboundUnboundUnbound
1qy6A01Unbound UnboundUnboundUnboundUnbound
2o8lA01Unbound UnboundUnboundUnboundUnbound
1wczA02Unbound UnboundUnboundUnboundUnbound
1qy6A02Unbound UnboundUnboundUnboundUnbound
2o8lA02Unbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [4] & Swiss-prot;P0C1U8, Q99V45
pdbCatalytic residuesMain-chain involved in catalysis
          
1wczA01SER 169
GLY 167;SER 169
1qy6A01SER 169
GLY 167;SER 169
2o8lA01SER 169
GLY 167;SER 169
1wczA02HIS 51;ASP 93
 
1qy6A02HIS 51;ASP 93
 
2o8lA02HIS 51;ASP 93
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Figure 5, p.4505-4508

references
[1]
PubMed ID4509307
JournalProc Natl Acad Sci U S A
Year1972
Volume69
Pages3506-9
AuthorsHoumard J, Drapeau GR
TitleStaphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds.
[2]
PubMed ID136253
JournalBiochem Biophys Res Commun
Year1976
Volume72
Pages411-7
AuthorsAusten BM, Smith EL
TitleAction of staphylococcal proteinase on peptides of varying chain length and composition.
[3]
PubMed ID12475199
JournalChem Rev
Year2002
Volume102
Pages4501-24
AuthorsHedstrom L
TitleSerine protease mechanism and specificity.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 69-342.
PubMed ID14747701
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages256-9
AuthorsPrasad L, Leduc Y, Hayakawa K, Delbaere LT
TitleThe structure of a universally employed enzyme: V8 protease from Staphylococcus aureus.
Related PDB1qy6,2o8l
Related UniProtKBQ99V45
[5]
PubMed ID17878159
JournalJ Biol Chem
Year2007
Volume282
Pages34129-38
AuthorsNickerson NN, Prasad L, Jacob L, Delbaere LT, McGavin MJ
TitleActivation 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.

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.

createdupdated
2011-02-242012-07-31
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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