ID   SFAS1_STRFR             Reviewed;         357 AA.
AC   Q03424;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine protease 1;
DE            EC=3.4.21.-;
DE   AltName: Full=Glutamic acid-specific protease;
DE   AltName: Full=SFase-1;
DE   Flags: Precursor;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC   STRAIN=ATCC 14544 / DSM 40758 / IMRU 3739 / NCIMB 11726 / NRRL B-2841;
RX   PubMed=8490047; DOI=10.1016/0167-4838(93)90176-r;
RA   Kitadokoro K., Nakamura E., Tamaki M., Horii T., Okamoto H., Shin M.,
RA   Sato T., Fujiwara T., Tsuzuki H., Yoshida N., Teraoka H.;
RT   "Purification, characterization and molecular cloning of an acidic amino
RT   acid-specific proteinase from Streptomyces fradiae ATCC 14544.";
RL   Biochim. Biophys. Acta 1163:149-157(1993).
RN   [2]
RP   3D-STRUCTURE MODELING.
RX   PubMed=7925392; DOI=10.1111/j.1432-1033.1994.00735.x;
RA   Kitadokoro K., Tsuzuki H., Okamoto H., Sato T.;
RT   "Crystal structure analysis of a serine proteinase from Streptomyces
RT   fradiae at 0.16-nm resolution and molecular modeling of an acidic-amino-
RT   acid-specific proteinase.";
RL   Eur. J. Biochem. 224:735-742(1994).
CC   -!- FUNCTION: Serine protease that preferentially cleaves peptide bonds on
CC       the C-terminal side of aspartate and glutamate with a 10-fold higher
CC       reactivity for a glutamyl bond than an aspartyl bond.
CC       {ECO:0000269|PubMed:8490047}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; D12470; BAA02038.1; -; Genomic_DNA.
DR   PIR; S33321; S33321.
DR   AlphaFoldDB; Q03424; -.
DR   SMR; Q03424; -.
DR   MEROPS; S01.267; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gene3D; 3.30.300.50; -; 1.
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; 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; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..170
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026917"
FT   CHAIN           171..357
FT                   /note="Serine protease 1"
FT                   /id="PRO_0000026918"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..204
FT                   /evidence="ECO:0000250"
FT   DISULFID        307..333
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  35849 MW;  B30364C40D906D2D CRC64;
     MRRTTRARTG LSALLLAASL GLGAAPAGAD APQRPAPTPA SDSAAALHAL DAAVERTLGD
     DSAGTYVDAG TGELVVTVTT EAAAAKVRAA GATPRRVQRG AAELDAAMAA LEARAKIPGT
     SWGLDPRTNR IAVEADSSVS ARDLARLRKV AASLDGAVSV TRVPGVFQRE VAGGDAIYGG
     GSRCSAAFNV TKNGVRYFLT AGHCTNLSST WSSTSGGTSI GVREGTSFPT NDYGIVRYTT
     TTNVDGRVNL YNGGYQDIAS AADAVVGQAI KKSGSTTKVT SGTVSAVNVT VNYSDGPVYG
     MVRTTACSAG GDSGGAHFAG SVALGIHSGS SGCTGTNGSA IHQPVREALS AYGVNVY