SSI_STRAO
ID SSI_STRAO Reviewed; 144 AA.
AC P01006;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Subtilisin inhibitor;
DE AltName: Full=SSI type;
DE Flags: Precursor;
GN Name=ssi;
OS Streptomyces albogriseolus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albogriseolus group.
OX NCBI_TaxID=1887;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S-3253;
RX PubMed=2732212; DOI=10.1093/oxfordjournals.jbchem.a122670;
RA Obata S., Taguchi S., Kumagai I., Miura K.;
RT "Molecular cloning and nucleotide sequence determination of gene encoding
RT Streptomyces subtilisin inhibitor (SSI).";
RL J. Biochem. 105:367-371(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Miura K., Kumagai I., Obata S., Kojima S., Taguchi S.;
RT "Partial alteration of a protein Streptomyces subtilisin inhibitor by site-
RT directed mutagenesis.";
RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:147-149(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-144.
RC STRAIN=S-3253;
RX PubMed=2482228; DOI=10.1016/0378-1119(89)90501-5;
RA Taguchi S., Nishiyama K., Kumagai I., Miura K.;
RT "Analysis of transcriptional control regions in the Streptomyces
RT subtilisin-inhibitor-encoding gene.";
RL Gene 84:279-286(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-144.
RX PubMed=8448204; DOI=10.1016/0167-4781(93)90212-v;
RA Ueda Y., Taguchi S., Nishiyama K., Kumagai I., Miura K.;
RT "Effect of a rare leucine codon, TTA, on expression of a foreign gene in
RT Streptomyces lividans.";
RL Biochim. Biophys. Acta 1172:262-266(1993).
RN [5]
RP PROTEIN SEQUENCE OF 32-144.
RC STRAIN=S-3253;
RX PubMed=4376147; DOI=10.1093/oxfordjournals.jbchem.a130672;
RA Ikenaka T., Odani S., Sakai M., Nabeshima Y., Sato S., Murao S.;
RT "Amino acid sequence of an alkaline proteinase inhibitor (Streptomyces
RT subtilisin inhibitor) from Streptomyces albogriseolus S-3253.";
RL J. Biochem. 76:1191-1209(1974).
RN [6]
RP SEQUENCE REVISION TO 142-143.
RX PubMed=6993452; DOI=10.1093/oxfordjournals.jbchem.a132819;
RA Sakai M., Odani S., Ikenaka T.;
RT "Importance of the carboxyl-terminal four amino acid residues in the
RT inhibitory activity of Streptomyces subtilisin inhibitor (with a revision
RT of its carboxyl-terminal sequence).";
RL J. Biochem. 87:891-898(1980).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=763329; DOI=10.1038/277447a0;
RA Mitsui Y., Satow Y., Watanabe Y., Hirono S., Iitaka Y.;
RT "Crystal structures of Streptomyces subtilisin inhibitor and its complex
RT with subtilisin BPN'.";
RL Nature 277:447-452(1979).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=6387152; DOI=10.1016/0022-2836(84)90150-5;
RA Hirono S., Akagawa H., Mitsui Y., Iitaka Y.;
RT "Crystal structure at 2.6-A resolution of the complex of subtilisin BPN'
RT with streptomyces subtilisin inhibitor.";
RL J. Mol. Biol. 178:389-413(1984).
RN [9]
RP MUTAGENESIS OF MET-104.
RX PubMed=1366538; DOI=10.1038/nbt0590-449;
RA Kojima S., Obata S., Kumagai I., Miura K.;
RT "Alteration of the specificity of the Streptomyces subtilisin inhibitor by
RT gene engineering.";
RL Biotechnology (N.Y.) 8:449-452(1990).
RN [10]
RP MUTAGENESIS OF MET-104.
RX PubMed=1908859; DOI=10.1093/oxfordjournals.jbchem.a123389;
RA Kojima S., Nishiyama Y., Kumagai I., Miura K.;
RT "Inhibition of subtilisin BPN' by reaction site P1 mutants of Streptomyces
RT subtilisin inhibitor.";
RL J. Biochem. 109:377-382(1991).
CC -!- FUNCTION: Strong inhibitor of bacterial serine proteases such as
CC subtilisin.
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; D00402; BAA00305.1; -; Genomic_DNA.
DR EMBL; M33133; AAA26821.1; -; Genomic_DNA.
DR EMBL; M33134; AAA26822.1; -; Genomic_DNA.
DR EMBL; X73049; CAA51525.1; -; Genomic_DNA.
DR EMBL; M54887; AAA26827.1; -; Genomic_DNA.
DR PIR; JX0066; XSSMA.
DR PDB; 2SIC; X-ray; 1.80 A; I=38-144.
DR PDB; 2TLD; X-ray; 2.60 A; I=35-144.
DR PDB; 3SIC; X-ray; 1.80 A; I=38-144.
DR PDB; 3SSI; X-ray; 2.30 A; A=32-144.
DR PDB; 5SIC; X-ray; 2.20 A; I=38-144.
DR PDBsum; 2SIC; -.
DR PDBsum; 2TLD; -.
DR PDBsum; 3SIC; -.
DR PDBsum; 3SSI; -.
DR PDBsum; 5SIC; -.
DR AlphaFoldDB; P01006; -.
DR SMR; P01006; -.
DR MINT; P01006; -.
DR MEROPS; I16.003; -.
DR EvolutionaryTrace; P01006; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:4376147"
FT CHAIN 32..144
FT /note="Subtilisin inhibitor"
FT /id="PRO_0000033270"
FT REPEAT 33..37
FT REPEAT 39..43
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 104..105
FT /note="Reactive bond for subtilisin"
FT DISULFID 66..81
FT DISULFID 102..132
FT MUTAGEN 104
FT /note="M->D,E,V,I,G,P: Decrease in inhibition."
FT /evidence="ECO:0000269|PubMed:1366538,
FT ECO:0000269|PubMed:1908859"
FT MUTAGEN 104
FT /note="M->K,R: Also inhibits trypsin."
FT /evidence="ECO:0000269|PubMed:1366538,
FT ECO:0000269|PubMed:1908859"
FT MUTAGEN 104
FT /note="M->Y,W: Also inhibits chymotrypsin."
FT /evidence="ECO:0000269|PubMed:1366538,
FT ECO:0000269|PubMed:1908859"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:2SIC"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3SSI"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2SIC"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2SIC"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2SIC"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:2SIC"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3SSI"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2SIC"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:2SIC"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:2SIC"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:2SIC"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2SIC"
SQ SEQUENCE 144 AA; 14312 MW; BEA57AC7FDCD8004 CRC64;
MRNTGAGPSP SVSRPPPSAA PLSGAALAAP GDAPSALYAP SALVLTVGKG VSATTAAPER
AVTLTCAPGP SGTHPAAGSA CADLAAVGGD LNALTRGEDV MCPMVYDPVL LTVDGVWQGK
RVSYERVFSN ECEMNAHGSS VFAF
