SSI12_STRHY
ID SSI12_STRHY Reviewed; 111 AA.
AC Q9R641;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Subtilisin inhibitor-like protein 12;
DE Short=SIL-12;
DE Short=SIL12;
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC STRAIN=ATCC 27438 / DSM 40578 / JCM 4772 / NBRC 13472 / NRRL 2387 /
RC M5-13184;
RX PubMed=8597568; DOI=10.1016/0167-4838(95)00207-3;
RA Terabe M., Kojima S., Taguchi S., Momose H., Miura K.;
RT "New subtilisin-trypsin inhibitors produced by Streptomyces: primary
RT structures and their relationship to other proteinase inhibitors from
RT Streptomyces.";
RL Biochim. Biophys. Acta 1292:233-240(1996).
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 PIR; S65720; S65720.
DR AlphaFoldDB; Q9R641; -.
DR SMR; Q9R641; -.
DR STRING; 68042.GCA_001553435_06428; -.
DR MEROPS; I16.013; -.
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.
FT CHAIN 1..111
FT /note="Subtilisin inhibitor-like protein 12"
FT /id="PRO_0000208663"
FT SITE 71..72
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT DISULFID 31..46
FT /evidence="ECO:0000250"
FT DISULFID 69..99
FT /evidence="ECO:0000250"
SQ SEQUENCE 111 AA; 11696 MW; 608204D09C7D0376 CRC64;
SLYPASALVL TVGHGADAAT AEVQRAVTLS CRPTPTGTHP APAQACAELH SVGGALGLLR
TGAEPGRMCT KEWRPITVTA EGVWDGRRVS YEHTFANNCF KNAAPTTVFE F