ID   PRTC_STRGR              Reviewed;         457 AA.
AC   P52320;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Streptogrisin-C;
DE            EC=3.4.21.-;
DE   AltName: Full=SGPC;
DE   AltName: Full=Serine protease C;
DE   Flags: Precursor;
GN   Name=sprC;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMRU 3499;
RX   PubMed=8051104; DOI=10.1016/s0021-9258(17)32141-5;
RA   Sidhu S.S., Kalmar G.B., Willis L.G., Borgford T.J.;
RT   "Streptomyces griseus protease C. A novel enzyme of the chymotrypsin
RT   superfamily.";
RL   J. Biol. Chem. 269:20167-20171(1994).
CC   -!- FUNCTION: Hydrolysis of proteins with specificity similar to
CC       chymotrypsin. May be specialized for the degradation of chitin-linked
CC       proteins. Has a primary specificity for large aliphatic or aromatic
CC       amino acids.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; L29018; AAA26813.1; -; Genomic_DNA.
DR   PIR; A53669; A53669.
DR   AlphaFoldDB; P52320; -.
DR   SMR; P52320; -.
DR   CAZy; CBM12; Carbohydrate-Binding Module Family 12.
DR   MEROPS; S01.265; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 3.30.300.50; -; 2.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
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; IPR035070; Streptogrisin_prodomain.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF02983; Pro_Al_protease; 1.
DR   PIRSF; PIRSF001134; Streptogrisin; 1.
DR   PRINTS; PR00861; ALYTICPTASE.
DR   SMART; SM00495; ChtBD3; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF51055; SSF51055; 1.
DR   PROSITE; PS51318; TAT; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Protease; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..34
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   PROPEP          35..202
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026913"
FT   CHAIN           203..457
FT                   /note="Streptogrisin-C"
FT                   /id="PRO_0000026914"
FT   DOMAIN          415..457
FT                   /note="Chitin-binding type-3"
FT   REGION          203..393
FT                   /note="Catalytic"
FT   REGION          393..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..413
FT                   /note="Linker"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT   ACT_SITE        266
FT                   /note="Charge relay system"
FT   ACT_SITE        347
FT                   /note="Charge relay system"
FT   DISULFID        219..239
FT                   /evidence="ECO:0000250"
FT   DISULFID        305..315
FT                   /evidence="ECO:0000250"
FT   DISULFID        341..368
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   457 AA;  46029 MW;  563A441560322209 CRC64;
     MERTTLRRRA LVAGTATVAV GALALAGLTG VASADPAATA APPVSADSLS PGMLAALERD
     LGLDEDAARS RIANEYRAAA VAAGLEKSLG ARYAGARVSG AKATLTVATT DASEAARITE
     AGARAEVVGH SLDRFEGVKK SLDKAALDKA PKNVPVWYVD VAANRVVVNA ASPAAGQAFL
     KVAGVDRGLV TVARSAEQPR ALADIRGGDA YYMNGSGRCS VGFSVTRGTQ NGFATAGHCG
     RVGTTTNGVN QQAQGTFQGS TFPGRDIAWV ATNANWTPRP LVNGYGRGDV TVAGSTASVV
     GASVCRSGST TGWHCGTIQQ LNTSVTYPEG TISGVTRTSV CAEPGDSGGS YISGSQAQGV
     TSGGSGNCSS GGTTYFQPIN PLLQAYGLTL VTSGGGTPTD PPTTPPTDSP GGTWAVGTAY
     AAGATVTYGG ATYRCLQAHT AQPGWTPADV PALWQRV