ID   GLUP_STRGR              Reviewed;         188 AA.
AC   Q07006;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glutamyl endopeptidase 2;
DE            EC=3.4.21.82;
DE   AltName: Full=GLUSGP;
DE   AltName: Full=Glutamic acid-specific protease;
DE   AltName: Full=Glutamyl endopeptidase II;
DE   AltName: Full=SGPE;
DE   AltName: Full=Serine protease E;
DE   AltName: Full=Streptogrisin-E;
GN   Name=sprE;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-121, AND PROTEIN SEQUENCE.
RC   STRAIN=IMRU 3499;
RX   PubMed=1959600; DOI=10.1016/0014-5793(91)80859-2;
RA   Svendsen I., Jensen M.R., Breddam K.;
RT   "The primary structure of the glutamic acid-specific protease of
RT   Streptomyces griseus.";
RL   FEBS Lett. 292:165-167(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1587264; DOI=10.1111/j.1432-1033.1992.tb16906.x;
RA   Breddam K., Meldal M.;
RT   "Substrate preferences of glutamic-acid-specific endopeptidases assessed by
RT   synthetic peptide substrates based on intramolecular fluorescence
RT   quenching.";
RL   Eur. J. Biochem. 206:103-107(1992).
RN   [3]
RP   3D-STRUCTURE MODELING.
RX   PubMed=8504858; DOI=10.1016/0014-5793(93)81529-9;
RA   Barbosa J.A.R.G., Garratt R.C., Saldanha J.W.;
RT   "A structural model for the glutamate-specific endopeptidase from
RT   Streptomyces griseus that explains substrate specificity.";
RL   FEBS Lett. 324:45-50(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=8105890; DOI=10.1021/bi00094a001;
RA   Nienaber V.L., Breddam K., Birktoft J.J.;
RT   "A glutamic acid specific serine protease utilizes a novel histidine triad
RT   in substrate binding.";
RL   Biochemistry 32:11469-11475(1993).
CC   -!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal
CC       side of glutamate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: -Glu-|-Xaa- >> -Asp-|-Xaa-. Preference
CC         for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-|-Asp- and
CC         -Glu-|-Pro- bonds is slow.; EC=3.4.21.82;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; S67853; AAB20424.2; -; Genomic_DNA.
DR   PDB; 1HPG; X-ray; 1.50 A; A=1-187.
DR   PDBsum; 1HPG; -.
DR   AlphaFoldDB; Q07006; -.
DR   SMR; Q07006; -.
DR   MEROPS; S01.267; -.
DR   EvolutionaryTrace; Q07006; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR001316; Pept_S1A_streptogrisin.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PRINTS; PR00861; ALYTICPTASE.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Serine protease.
FT   CHAIN           1..188
FT                   /note="Glutamyl endopeptidase 2"
FT                   /id="PRO_0000093856"
FT   ACT_SITE        33
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        62
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..34
FT   DISULFID        137..163
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          99..104
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          108..123
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          126..134
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          152..161
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:1HPG"
FT   HELIX           175..182
FT                   /evidence="ECO:0007829|PDB:1HPG"
SQ   SEQUENCE   188 AA;  18337 MW;  2762E5FDB2FD368D CRC64;
     VLGGGAIYGG GSRCSAAFNV TKGGARYFVT AGHCTNISAN WSASSGGSVV GVREGTSFPT
     NDYGIVRYTD GSSPAGTVDL YNGSTQDISS AANAVVGQAI KKSGSTTKVT SGTVTAVNVT
     VNYGDGPVYN MGRTTACSAG GDSGGAHFAG SVALGIHSGS SGCSGTAGSA IHQPVTKALS
     AYGVTVYL