ID   PRTD_STRGR              Reviewed;         392 AA.
AC   P52321;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Streptogrisin-D;
DE            EC=3.4.21.-;
DE   AltName: Full=SGPD;
DE   AltName: Full=Serine protease D;
DE   Flags: Precursor;
GN   Name=sprD;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=IMRU 3499;
RX   PubMed=7706307; DOI=10.1074/jbc.270.13.7594;
RA   Sidhu S.S., Kalmar G.B., Willis L.G., Borgford T.J.;
RT   "Protease evolution in Streptomyces griseus. Discovery of a novel dimeric
RT   enzymes.";
RL   J. Biol. Chem. 270:7594-7600(1995).
CC   -!- FUNCTION: Has a primary specificity for large aliphatic or aromatic
CC       amino acids.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; L29019; AAA74409.1; -; Genomic_DNA.
DR   PIR; A56123; A56123.
DR   AlphaFoldDB; P52321; -.
DR   SMR; P52321; -.
DR   MEROPS; S01.266; -.
DR   OMA; MKHRRIP; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; IPR004236; Pept_S1_alpha_lytic.
DR   InterPro; IPR001316; Pept_S1A_streptogrisin.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF02983; Pro_Al_protease; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001134; Streptogrisin; 1.
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   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..64
FT                   /evidence="ECO:0000255"
FT   PROPEP          65..204
FT                   /id="PRO_0000026915"
FT   CHAIN           205..392
FT                   /note="Streptogrisin-D"
FT                   /id="PRO_0000026916"
FT   ACT_SITE        237
FT                   /note="Charge relay system"
FT   ACT_SITE        266
FT                   /note="Charge relay system"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT   DISULFID        218..238
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..369
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  40113 MW;  6F699E026BF1D6A5 CRC64;
     MCVSRRRNSG RPILRVRAPH LLRARPHRRS KLKHRRISRK RATLAGSAVV ALVAAGFTFQ
     TANASDDVPA FGAKTLSADA AGKLATTLDR DLGADAAGSY YDATAKTLVV NVVDEAGAEQ
     VRQAGGKARI VENSLAELKS ARGTLTEKAT IPGTSWAVDP VSNKVLVTAD STVDGAAWKK
     LSAVVEGLGG KAELNRTAGE FTPLIAGGDA IWGSGSRCSL GFNVVKGGEP YFLTAGHCTE
     SVTSWSDTQG GSEIGANEGS SFPENDYGLV KYTSDTAHPS EVNLYDGSTQ AITQAGDATV
     GQAVTRSGST TQVHDGEVTA LDATVNYGNG DIVNGLIQTT VCAEPGDSGG ALFAGDTALG
     LTSGGSGDCS SGGTTFFQPV PEALAAYGAE IG