NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 67-85, FUNCTION, ENZYME REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55;
DOI=10.1006/mpat.2002.0515; PubMed=12127798 [NCBI, ExPASy, EBI, Israel, Japan]
Ohara-Nemoto Y., Ikeda Y., Kobayashi M., Sasaki M., Tajika S., Kimura S.;
"Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis.";
Microb. Pathog. 33:33-41(2002).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-282, AND PROTEIN SEQUENCE OF 67-96.
STRAIN=6746;
DOI=10.1515/BC.2001.192; PubMed=11767947 [NCBI, ExPASy, EBI, Israel, Japan]
Dubin G., Chmiel D., Mak P., Rakwalska M., Rzychon M., Dubin A.;
"Molecular cloning and biochemical characterisation of proteases from Staphylcoccus epidermidis.";
Biol. Chem. 382:1575-1582(2001).

Comments

FUNCTION: Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen.
CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
ENZYME REGULATION: Inhibited by diisopropyl fluorophosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8.0. Active from pH 6.0 to 9.0;
SUBUNIT: Monomer (Probable).
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the peptidase S1B family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB096695; BAC24763.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ305145; CAC27157.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P09332; 1DT2. [HSSP ENTRY / PDB]

ModBase

P0C0Q1.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000126; Pept_S1B_AS.
IPR001254; Peptidase_S1_S6.
IPR008256; Peptidase_S1B.
IPR008353; Peptidase_S1B_tx.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR01774; EXFOLTOXIN.
PR00839; V8PROTEASE.

PROSITE

PS00672; V8_HIS; FALSE_NEG.
PS00673; V8_SER; 1.

Other

ProtoNet

P0C0Q1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease; Signal; Virulence; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 27`	`27`	`Potential.`
`PROPEP`	`28 66`	`39`		`PRO_0000026896`
`CHAIN`	`67 282`	`216`	`Glutamyl endopeptidase.`	`PRO_0000026897`
`ACT_SITE`	`117 117`		`Charge relay system (By similarity).`
`ACT_SITE`	`159 159`		`Charge relay system (By similarity).`
`ACT_SITE`	`235 235`		`Charge relay system (By similarity).`

Sequence information

Length: 282 AA [This is the length of the unprocessed precursor]

Molecular weight: 30809 Da [This is the MW of the unprocessed precursor]

CRC64: 5DAD3E8D7EB3E0CB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKRFLSICT MTIAALATTT MVNTSYAKTD TESHNHSSLG TENKNVLDIN SSSHNIKPSQ 

        70         80         90        100        110        120 
NKSYPSVILP NNNRHQIFNT TQGHYDAVSF IYIPIDGGYM SGSGVVVGEN EILTNKHVVN 

       130        140        150        160        170        180 
GAKGNPRNIS VHPSAKNEND YPNGKFVGQE IIPYPGNSDL AILRVSPNEH NQHIGQVVKP 

       190        200        210        220        230        240 
ATISSNTDTR INENITVTGY PGDKPLATMW ESVGKVVYIG GEELRYDLST VGGNSGSPVF 

       250        260        270        280 
NGKNQVIGIH YGGVDNKYNS SVYINDFVQQ FLRNNIPDIN IQ

P0C0Q1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools