ID   SFAS2_STRFR             Reviewed;         174 AA.
AC   P41140;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Serine protease 2;
DE            EC=3.4.21.-;
DE   AltName: Full=SFase-2;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14544 / DSM 40758 / IMRU 3739 / NCIMB 11726 / NRRL B-2841;
RX   PubMed=8119298; DOI=10.1111/j.1432-1033.1994.tb18598.x;
RA   Kitadokoro K., Tsuzuki H., Nakamura E., Sato T., Teraoka H.;
RT   "Purification, characterization, primary structure, crystallization and
RT   preliminary crystallographic study of a serine proteinase from Streptomyces
RT   fradiae ATCC 14544.";
RL   Eur. J. Biochem. 220:55-61(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RC   STRAIN=ATCC 14544 / DSM 40758 / IMRU 3739 / NCIMB 11726 / NRRL B-2841;
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: Broad substrate specificity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; S68947; AAB30080.2; -; Genomic_DNA.
DR   PDB; 2SFA; X-ray; 1.60 A; A=1-174.
DR   PDBsum; 2SFA; -.
DR   AlphaFoldDB; P41140; -.
DR   SMR; P41140; -.
DR   MEROPS; S01.431; -.
DR   EvolutionaryTrace; P41140; -.
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   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; PF00089; Trypsin; 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   3D-structure; Disulfide bond; Hydrolase; Protease; Secreted;
KW   Serine protease.
FT   CHAIN           1..174
FT                   /note="Serine protease 2"
FT                   /id="PRO_0000093857"
FT   ACT_SITE        35
FT                   /note="Charge relay system"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT   DISULFID        15..36
FT   DISULFID        141..168
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          19..23
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   HELIX           34..37
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          66..72
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          111..125
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          131..139
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          156..167
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   TURN            168..170
FT                   /evidence="ECO:0007829|PDB:2SFA"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:2SFA"
SQ   SEQUENCE   174 AA;  17179 MW;  240BF8B84AC572EA CRC64;
     IAGGEAIYAA GGGRCSLGFN VRSSSGATYA LTAGHCTEIA STWYTNSGQT SLLGTRAGTS
     FPGNDYGLIR HSNASAADGR VYLYNGSYRD ITGAGNAYVG QTVQRSGSTT GLHSGRVTGL
     NATVNYGGGD IVSGLIQTNV CAEPGDSGGA LFAGSTALGL TSGGSGNCRT GGTT