ID   SSI_STRFR               Reviewed;         142 AA.
AC   Q9ZA15;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   12-AUG-2020, entry version 67.
DE   RecName: Full=Subtilase-type protease inhibitor;
DE   Flags: Precursor;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SMF9;
RA   Lee K.J.;
RT   "Molecular cloning of serine protease inhibitor Streptomyces fradiae
RT   SMF9.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD09245.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U90533; AAD09245.2; ALT_FRAME; Genomic_DNA.
DR   STRING; 1906.SFRA_31995; -.
DR   eggNOG; ENOG50333FU; Bacteria.
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; IPR023549; Subtilisin_inhibitor.
DR   InterPro; IPR036819; Subtilisin_inhibitor-like_sf.
DR   Pfam; PF00720; SSI; 1.
DR   PRINTS; PR00294; SSBTLNINHBTR.
DR   SUPFAM; SSF55399; SSF55399; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..142
FT                   /note="Subtilase-type protease inhibitor"
FT                   /id="PRO_0000033273"
FT   SITE            67..68
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        100..130
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   142 AA;  14712 MW;  303C37BDD4AFF97A CRC64;
     MRNRAKTALV GTLVAATAAL GPLGGTAHAG DSSLYAPSDL VLTIAHGEDA ASVAPERAVT
     LTCEPQARGT HPSPQEACVL LGDAGGDVDA IAPPAEPQLC TYQYDPVVVT CXGVWQGRFV
     DQERTFGNEC VMRAETGAVF DF