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   16-JUN-2009, entry version 69.
DE   RecName: Full=Glutamyl endopeptidase 2;
DE            EC=3.4.21.82;
DE   AltName: Full=Glutamyl endopeptidase II;
DE   AltName: Full=Glutamic acid-specific protease;
DE   AltName: Full=GLUSGP;
DE   AltName: Full=Streptogrisin-E;
DE   AltName: Full=Serine protease E;
DE   AltName: Full=SGPE;
GN   Name=sprE;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-121, AND PROTEIN SEQUENCE.
RC   STRAIN=IMRU 3499;
RX   MEDLINE=92070480; 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
RT   assessed by synthetic peptide substrates based on intramolecular
RT   fluorescence quenching.";
RL   Eur. J. Biochem. 206:103-107(1992).
RN   [3]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE=93279375; 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   MEDLINE=94032266; 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
RT   triad in substrate binding.";
RL   Biochemistry 32:11469-11475(1993).
CC   -!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-
CC       terminal side of glutamate.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: -Glu-|-Xaa- >> -Asp-|-
CC       Xaa-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of
CC       -Glu-|-Asp- and -Glu-|-Pro- bonds is slow.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
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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   MEROPS; S01.267; -.
DR   BRENDA; 3.4.21.82; 1270.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001316; Pept_S1A_streptogrisin.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00861; ALYTICPTASE.
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       Glutamyl endopeptidase 2.
FT                                /FTId=PRO_0000093856.
FT   ACT_SITE     33     33       Charge relay system (By similarity).
FT   ACT_SITE     62     62       Charge relay system (By similarity).
FT   ACT_SITE    143    143       Charge relay system (By similarity).
FT   DISULFID     14     34
FT   DISULFID    137    163
FT   STRAND        6      9
FT   STRAND       12     15
FT   STRAND       18     22
FT   STRAND       25     30
FT   HELIX        32     35
FT   STRAND       39     44
FT   STRAND       49     57
FT   STRAND       59     61
FT   STRAND       63     68
FT   STRAND       76     79
FT   STRAND       81     83
FT   STRAND       85     87
FT   STRAND       99    104
FT   TURN        105    107
FT   STRAND      108    123
FT   STRAND      126    134
FT   STRAND      146    149
FT   STRAND      152    161
FT   STRAND      171    174
FT   HELIX       175    182
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
//