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Reviewed, UniProtKB/Swiss-Prot P0C0Q1 (GSEA_STAEP)

Last modified January 19, 2010. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl endopeptidase
    EC=3.4.21.19
Alternative name(s):
    Glutamic acid-specific protease
      Short name=GluSE
Gene names
Name: gseA
Synonyms: esp
OrganismStaphylococcus epidermidis
Taxonomic identifier1282 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen. Ref.1

Catalytic activity

Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.

Enzyme regulation

Inhibited by diisopropyl fluorophosphate. Ref.1

Subunit structure

Monomer Probable. Ref.1

Subcellular location

Secreted Ref.1.

Sequence similarities

Belongs to the peptidase S1B family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0. Active from pH 6.0 to 9.0.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMZymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 6639
PRO_0000026896
Chain67 – 282216Glutamyl endopeptidase
PRO_0000026897

Sites

Active site1171Charge relay system By similarity
Active site1591Charge relay system By similarity
Active site2351Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C0Q1-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 5DAD3E8D7EB3E0CB

FASTA28230,809
        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 

« Hide

References

[1]"Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis."
Ohara-Nemoto Y., Ikeda Y., Kobayashi M., Sasaki M., Tajika S., Kimura S.
Microb. Pathog. 33:33-41(2002) [PubMed: 12127798] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 67-85, FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
Strain: ATCC 14990 / DSM 20044 / CIP 81.55.
[2]"Molecular cloning and biochemical characterisation of proteases from Staphylcoccus epidermidis."
Dubin G., Chmiel D., Mak P., Rakwalska M., Rzychon M., Dubin A.
Biol. Chem. 382:1575-1582(2001) [PubMed: 11767947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-282, PROTEIN SEQUENCE OF 67-96.
Strain: 6746.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB096695 Genomic DNA. Translation: BAC24763.1.
AJ305145 Genomic DNA. Translation: CAC27157.1.

3D structure databases

SMRP0C0Q1. Positions 67-281.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.4.21.19. 874.

Family and domain databases

InterProIPR000126. Pept_S1B_AS.
IPR001254. Peptidase_S1_S6.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
PROSITEPS00672. V8_HIS. False negative.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSEA_STAEP
AccessionPrimary (citable) accession number: P0C0Q1
Secondary accession number(s): Q7DG19, Q8CMC1, Q9AJX0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: January 19, 2010
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents