ID   TRYP_STRGA              Reviewed;         268 AA.
AC   Q54179;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Trypsin-like protease;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Streptomyces glaucescens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RA   Hintermann G.;
RT   "Cloning, partial characterization and nucleotide sequence of a trypsin-
RT   like protease gene from Streptomyces glaucescens.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protease that shows preferential cleavage after Arg and Lys
CC       residues.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; U13770; AAA21336.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54179; -.
DR   SMR; Q54179; -.
DR   STRING; 1907.SGLAU_09150; -.
DR   MEROPS; S01.101; -.
DR   eggNOG; COG5640; Bacteria.
DR   OMA; HEAEVHY; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Protease; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   PROPEP          42..45
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028303"
FT   CHAIN           46..268
FT                   /note="Trypsin-like protease"
FT                   /id="PRO_0000028304"
FT   DOMAIN          46..266
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        82
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        127
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        217
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            211
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        187..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        213..242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   268 AA;  27551 MW;  01D05E0A4D5D177A CRC64;
     MTHTTTIAAK RGGLALAKKA AAAGAVALAV ASLQPVSAAH AADARVIGGK PAAQNEFPFM
     VHLSMGCGGA LYKKDIVLTA AHCMDGSGNN TRITVTAGVA DLNSSGAIKV KSTKVKVAPG
     YDGVGKDWAL IKLAKPIDRP TLKIATTAKY NRGTFTIAGW GDVREGAGTG TTKLQKANVP
     FVSDRACKWH YGNRLVPKQE LCAGYASGGI DTCQGDSGGP MFRKDDAGKW IQVGIVSWGD
     GCARSGVPGV YTEVSTFAKD IAKAASAL