Q07006 (GLUP_STRGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Streptomyces griseus

Taxonomic identifier

1911 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Hydrolase Protease Serine protease
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 188

188

Glutamyl endopeptidase 2

PRO_0000093856

Sites

Active site

33

1

Charge relay system By similarity

Active site

62

1

Charge relay system By similarity

Active site

143

1

Charge relay system By similarity

Amino acid modifications

Disulfide bond

14 ↔ 34

Disulfide bond

137 ↔ 163

Secondary structure

1

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188

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Beta strand

12 – 15

4

Beta strand

18 – 22

5

Beta strand

25 – 30

6

Helix

32 – 35

4

Beta strand

39 – 44

6

Beta strand

49 – 57

9

Beta strand

59 – 61

3

Beta strand

63 – 68

6

Beta strand

76 – 79

4

Beta strand

81 – 83

3

Beta strand

85 – 87

3

Beta strand

99 – 104

6

Turn

105 – 107

3

Beta strand

108 – 123

16

Beta strand

126 – 134

9

Beta strand

146 – 149

4

Beta strand

152 – 161

10

Beta strand

171 – 174

4

Helix

175 – 182

8

Sequences

	Sequence		Length	Mass (Da)
	Q07006 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 2762E5FDB2FD368D	FASTA	188	18,337
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HPG	X-ray	1.50	A	1-187	[»]

ProteinModelPortal

Q07006.

SMR

Q07006. Positions 1-187.

ModBase

Search...

Protein family/group databases

MEROPS

S01.267.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR009003. Pept_cys/ser_Trypsin-like.
IPR001316. Pept_S1A_streptogrisin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00861. ALYTICPTASE.

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLUP_STRGR

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program