ID   TRYP_STREX              Reviewed;         260 AA.
AC   P80420; Q6U1K3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Trypsin-like protease;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=tlp;
OS   Streptomyces exfoliatus (Streptomyces hydrogenans).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SMF13;
RA   Lee D.H., Kim Y.-H., Kim I.S., Lee K.J.;
RT   "Role of trypsin-like protease on morphological differentiation of
RT   Streptomyces exfoliatus SMF13.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 39-58.
RC   STRAIN=SMF13;
RX   PubMed=7773379; DOI=10.1099/13500872-141-4-1017;
RA   Kim I.S., Lee K.J.;
RT   "Physiological roles of leupeptin and extracellular proteases in mycelium
RT   development of Streptomyces exfoliatus SMF13.";
RL   Microbiology 141:1017-1025(1995).
CC   -!- FUNCTION: Involved in mycelium differentiation.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AY380806; AAQ88430.1; -; Genomic_DNA.
DR   AlphaFoldDB; P80420; -.
DR   SMR; P80420; -.
DR   MEROPS; S01.101; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..38
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:7773379"
FT                   /id="PRO_0000028305"
FT   CHAIN           39..260
FT                   /note="Trypsin-like protease"
FT                   /id="PRO_0000028306"
FT   DOMAIN          39..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        179..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        39
FT                   /note="V -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="E -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53..54
FT                   /note="MV -> QQ (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  26593 MW;  9B56032D44F8490B CRC64;
     MLTVTTLVQL MKRTLAVGAV ALAAVSLQPG TATAGPAPVV GGTRAAQGEF PFMVRLSMGC
     GGALYTQQIV LTAAHCVSGS GNNTSITATA GVVDLNSSSA IKVKSTKVLQ APGYNGKGKD
     WALIKLAKPI NLPTLKIADT KAYDNGTFTV AGWGAAREGG GQQRYLLKAN VPFVSDASCQ
     SSYGSDLVPS EEICAGLPQG GVDTCQGDSG GPMFRRDNNN AWIQVGIVSW GEGCARPNYP
     GVYTEVSTFA AAIKSAAAGM