ID   SSI_STRAW               Reviewed;         144 AA.
AC   Q825H1;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Probable subtilase-type protease inhibitor;
DE   Flags: Precursor;
GN   Name=sti1; OrderedLocusNames=SAV_7486;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- FUNCTION: Strong inhibitor of bacterial serine proteases such as
CC       subtilisin. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family.
CC       {ECO:0000305}.
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DR   EMBL; BA000030; BAC75197.1; -; Genomic_DNA.
DR   RefSeq; WP_010988881.1; NZ_JZJK01000065.1.
DR   AlphaFoldDB; Q825H1; -.
DR   SMR; Q825H1; -.
DR   STRING; 227882.SAV_7486; -.
DR   MEROPS; I16.001; -.
DR   EnsemblBacteria; BAC75197; BAC75197; SAVERM_7486.
DR   KEGG; sma:SAVERM_7486; -.
DR   eggNOG; ENOG50333FU; Bacteria.
DR   HOGENOM; CLU_121949_0_0_11; -.
DR   OMA; TFANECV; -.
DR   OrthoDB; 2050426at2; -.
DR   Proteomes; UP000000428; Chromosome.
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   3: Inferred from homology;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..144
FT                   /note="Probable subtilase-type protease inhibitor"
FT                   /id="PRO_0000033271"
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;  14716 MW;  CFC7F7A43B9EC18D CRC64;
     MPNTARWAVT LTLTATAVCG PLAGASLATP NAAASGLYAP SALVLTTGHG QSAATATPER
     AVTLNCAPTA SGTHPAAVSA CAELRATGGD FDALSARSDA MCTRQYDPVV VTVEGVWQGK
     RVAYERTFAN ECVKNSYGTT VFTF