ID   SSIT_STRMB              Reviewed;         148 AA.
AC   P83544; N1NVD6;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Transglutaminase-activating metalloprotease inhibitor;
DE            Short=TAMEP inhibitor;
DE   AltName: Full=P14;
DE   Flags: Precursor;
GN   Name=sti;
OS   Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=35621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 /
RC   NRRL B-3729 / VKM Ac-928;
RA   Zindel S., Froels S., Kletzin A., Pfeifer F., Fuchsbauer H.L.;
RT   "Gene structure of the subtilisin and transglutaminase-activating
RT   metalloprotease inhibitor from Streptomyces mobaraensis.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 39-54, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 27441 / CBS 777.72 / DSM 40587 / JCM 4778 / NBRC 13476 / VKM
RC   Ac-879;
RX   PubMed=12869197; DOI=10.1046/j.1432-1033.2003.03703.x;
RA   Zotzel J., Keller P., Fuchsbauer H.-L.;
RT   "Transglutaminase from Streptomyces mobaraensis is activated by an
RT   endogenous metalloprotease.";
RL   Eur. J. Biochem. 270:3214-3222(2003).
CC   -!- FUNCTION: Inhibits transglutaminase-activating metalloprotease.
CC       {ECO:0000269|PubMed:12869197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12869197}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HF968451; CCW72533.1; -; Genomic_DNA.
DR   PDB; 6I0I; X-ray; 1.45 A; A/B=41-148.
DR   PDBsum; 6I0I; -.
DR   AlphaFoldDB; P83544; -.
DR   SMR; P83544; -.
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; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000269|PubMed:12869197"
FT   CHAIN           39..148
FT                   /note="Transglutaminase-activating metalloprotease
FT                   inhibitor"
FT                   /id="PRO_0000208666"
FT   SITE            108..109
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..136
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39
FT                   /note="S -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="G -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          45..55
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   STRAND          59..68
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   HELIX           80..89
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   HELIX           94..98
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   STRAND          113..121
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   STRAND          124..134
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   HELIX           135..141
FT                   /evidence="ECO:0007829|PDB:6I0I"
FT   TURN            143..146
FT                   /evidence="ECO:0007829|PDB:6I0I"
SQ   SEQUENCE   148 AA;  15170 MW;  6B4E5F5F38DAF777 CRC64;
     MRYITGGIAL GSALILGSLV GAGATASATP APAPAAQQSL YAPSALVLTV GQGDKAASAG
     VQRAVTLNCM PKPSGTHPDA RGACDQLRAA SGNFAEITKI KSGTACTKEW NPFVVTAEGV
     WEGQRVKYEH TFANPCEMKA GKGTVFEF