ID   SSI_STRLI               Reviewed;         144 AA.
AC   P61153; P28591; Q9R644;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Protease inhibitor;
DE   AltName: Full=SILA-3;
DE   AltName: Full=SLPI;
DE   AltName: Full=Trypsin inhibitor STI1;
DE   Flags: Precursor;
GN   Name=sti1;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-85; 87-103
RP   AND 105-143.
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 38-144.
RC   STRAIN=66 / 1326;
RX   PubMed=1356971; DOI=10.1093/oxfordjournals.jbchem.a123878;
RA   Ueda Y., Kojima S., Tsumoto K., Takeda S., Miura K., Kumagai I.;
RT   "A protease inhibitor produced by Streptomyces lividans 66 exhibits
RT   inhibitory activities toward both subtilisin BPN' and trypsin.";
RL   J. Biochem. 112:204-211(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 36-71.
RC   STRAIN=66 / 1326;
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: Strong inhibitory activity toward subtilisin BPN' and, to a
CC       lesser extent, toward trypsin.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family.
CC       {ECO:0000305}.
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DR   EMBL; M80576; AAA26801.1; -; Genomic_DNA.
DR   PIR; B42585; B42585.
DR   AlphaFoldDB; P61153; -.
DR   SMR; P61153; -.
DR   MEROPS; I16.007; -.
DR   MEROPS; I16.008; -.
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..35
FT                   /evidence="ECO:0000269|PubMed:1737780,
FT                   ECO:0000269|PubMed:7763545"
FT   CHAIN           36..144
FT                   /note="Protease inhibitor"
FT                   /id="PRO_0000033274"
FT   SITE            104..105
FT                   /note="Reactive bond"
FT   DISULFID        66..81
FT   DISULFID        102..132
SQ   SEQUENCE   144 AA;  14433 MW;  E748BADF078A4F8B CRC64;
     MRNTARWAAT LGLTATAVCG PLAGASLASP ATAPASLYAP SALVLTVGHG ESAATAAPLR
     AVTLTCAPTA SGTHPAAAAA CAELRAAHGD PSALAAEDSV MCTREYAPVV VTVDGVWQGR
     RLSYERTFAN ECVKNAGSAS VFTF