ID   SSI2_STRLO              Reviewed;         144 AA.
AC   P35706;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Trypsin inhibitor STI2;
DE   Flags: Precursor;
GN   Name=sti2;
OS   Streptomyces longisporus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1737780; DOI=10.1016/s0021-9258(19)50721-9;
RA   Strickler J.E., Berka T.R., Gorniak J., Fornwald J., Keys R., Rowland J.J.,
RA   Rosenberg M., Taylor D.P.;
RT   "Two novel Streptomyces protein protease inhibitors. Purification,
RT   activity, cloning, and expression.";
RL   J. Biol. Chem. 267:3236-3241(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 35-71.
RC   STRAIN=4395;
RX   PubMed=7763545; DOI=10.1271/bbb.57.522;
RA   Taguchi S., Kikuchi H., Kojima S., Kumagai I., Nakase T., Miura K.,
RA   Momose H.;
RT   "High frequency of SSI-like protease inhibitors among Streptomyces.";
RL   Biosci. Biotechnol. Biochem. 57:522-524(1993).
CC   -!- FUNCTION: Inhibitory activity against trypsin.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family.
CC       {ECO:0000305}.
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DR   EMBL; M80577; AAA26802.1; -; Genomic_DNA.
DR   PIR; A42585; A42585.
DR   AlphaFoldDB; P35706; -.
DR   SMR; P35706; -.
DR   MEROPS; I16.006; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.350.10; -; 1.
DR   HAMAP; MF_00778; SSI; 1.
DR   InterPro; IPR000691; Prot_inh_I16_SSI.
DR   InterPro; IPR020054; Prot_inh_SSI_I16_CS.
DR   InterPro; IPR023549; Subtilisin_inhibitor.
DR   InterPro; IPR036819; Subtilisin_inhibitor-like_sf.
DR   Pfam; PF00720; SSI; 1.
DR   PRINTS; PR00294; SSBTLNINHBTR.
DR   SUPFAM; SSF55399; SSF55399; 1.
DR   PROSITE; PS00999; SSI; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000269|PubMed:7763545"
FT   CHAIN           35..144
FT                   /note="Trypsin inhibitor STI2"
FT                   /id="PRO_0000033275"
FT   SITE            104..105
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..132
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   144 AA;  14548 MW;  BBE9A46B67E8F1C6 CRC64;
     MRNTARWAAT LALTATAVCG PLTGAALATP AAAPASLYAP SALVLTVGHG TSAAAASPLR
     AVTLNCAPTA SGTHPAPALA CADLRGVGGD IDALKARDGV ICNKLYDPVV VTVDGVWQGK
     RVSYERTFGN ECVKNSYGTS LFAF