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Q07006 (GLUP_STRGR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl endopeptidase 2

EC=3.4.21.82
Alternative name(s):
GLUSGP
Glutamic acid-specific protease
Glutamyl endopeptidase II
SGPE
Serine protease E
Streptogrisin-E
Gene names
Name:sprE
OrganismStreptomyces griseus
Taxonomic identifier1911 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Preferentially cleaves peptide bonds on the carboxyl-terminal side of glutamate.

Catalytic activity

Preferential cleavage: -Glu-|-Xaa- >> -Asp-|-Xaa-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-|-Asp- and -Glu-|-Pro- bonds is slow.

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase S1 family.

Ontologies

Keywords
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Chain1 – 188188Glutamyl endopeptidase 2
PRO_0000093856

Sites

Active site331Charge relay system By similarity
Active site621Charge relay system By similarity
Active site1431Charge relay system By similarity

Amino acid modifications

Disulfide bond14 ↔ 34
Disulfide bond137 ↔ 163

Secondary structure

...................................... 188
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07006 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 2762E5FDB2FD368D

FASTA18818,337
        10         20         30         40         50         60 
VLGGGAIYGG GSRCSAAFNV TKGGARYFVT AGHCTNISAN WSASSGGSVV GVREGTSFPT 

        70         80         90        100        110        120 
NDYGIVRYTD GSSPAGTVDL YNGSTQDISS AANAVVGQAI KKSGSTTKVT SGTVTAVNVT 

       130        140        150        160        170        180 
VNYGDGPVYN MGRTTACSAG GDSGGAHFAG SVALGIHSGS SGCSGTAGSA IHQPVTKALS 


AYGVTVYL 

« Hide

References

[1]"The primary structure of the glutamic acid-specific protease of Streptomyces griseus."
Svendsen I., Jensen M.R., Breddam K.
FEBS Lett. 292:165-167(1991) [PubMed: 1959600] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-121, PROTEIN SEQUENCE.
Strain: IMRU 3499.
[2]"Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching."
Breddam K., Meldal M.
Eur. J. Biochem. 206:103-107(1992) [PubMed: 1587264] [Abstract]
Cited for: CHARACTERIZATION.
[3]"A structural model for the glutamate-specific endopeptidase from Streptomyces griseus that explains substrate specificity."
Barbosa J.A.R.G., Garratt R.C., Saldanha J.W.
FEBS Lett. 324:45-50(1993) [PubMed: 8504858] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[4]"A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding."
Nienaber V.L., Breddam K., Birktoft J.J.
Biochemistry 32:11469-11475(1993) [PubMed: 8105890] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S67853 Genomic DNA. Translation: AAB20424.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HPGX-ray1.50A1-187[»]
ProteinModelPortalQ07006.
SMRQ07006. Positions 1-187.
ModBaseSearch...

Protein family/group databases

MEROPSS01.267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR001316. Pept_S1A_streptogrisin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00861. ALYTICPTASE.
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLUP_STRGR
AccessionPrimary (citable) accession number: Q07006
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 16, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families