ID   IMEP_STRNI              Reviewed;         131 AA.
AC   P01077;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Metalloproteinase inhibitor;
DE   Flags: Precursor;
GN   Name=smpI;
OS   Streptomyces nigrescens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2243793; DOI=10.1093/nar/18.21.6433;
RA   Tanaka K., Aoki H., Oda K., Murao S., Saito H., Takahashi H.;
RT   "Nucleotide sequence of the gene for a metalloproteinase inhibitor of
RT   Streptomyces nigrescens (SMPI).";
RL   Nucleic Acids Res. 18:6433-6433(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 30-131, AND DISULFIDE BONDS.
RC   STRAIN=TK-23;
RX   PubMed=3888972; DOI=10.1093/oxfordjournals.jbchem.a135041;
RA   Murai H., Hara S., Ikenaka T., Oda K., Murao S.;
RT   "Amino acid sequence of Streptomyces metallo-proteinase inhibitor from
RT   Streptomyces nigrescens TK-23.";
RL   J. Biochem. 97:173-180(1985).
RN   [3]
RP   STRUCTURE BY NMR.
RC   STRAIN=TK-23;
RX   PubMed=9735297; DOI=10.1006/jmbi.1998.2022;
RA   Ohno A., Tate S., Seeram S.S., Hiraga K., Swindells M.B., Oda K.,
RA   Kainosho M.;
RT   "NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI,
RT   isolated from Streptomyces nigrescens TK-23: another example of an
RT   ancestral beta gamma-crystallin precursor structure.";
RL   J. Mol. Biol. 282:421-433(1998).
CC   -!- FUNCTION: Inhibits microbial metallo-proteinases, such as thermolysin,
CC       but not serine, thiol, or carboxyl proteinases.
CC   -!- MISCELLANEOUS: Thermolysin slowly cleaves only the peptide bond
CC       following Cys-93.
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DR   EMBL; D00671; BAA00574.1; -; Genomic_DNA.
DR   PIR; S12615; ZYSMN.
DR   PDB; 1BHU; NMR; -; A=30-131.
DR   PDBsum; 1BHU; -.
DR   AlphaFoldDB; P01077; -.
DR   BMRB; P01077; -.
DR   SMR; P01077; -.
DR   MEROPS; I36.001; -.
DR   EvolutionaryTrace; P01077; -.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.20.30; -; 1.
DR   InterPro; IPR015791; Antimic/Inh_G_crystallin-like.
DR   InterPro; IPR011024; G_crystallin-like.
DR   SUPFAM; SSF49695; SSF49695; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:3888972"
FT   CHAIN           30..131
FT                   /note="Metalloproteinase inhibitor"
FT                   /id="PRO_0000021509"
FT   DISULFID        33..39
FT                   /evidence="ECO:0000269|PubMed:3888972"
FT   DISULFID        93..98
FT                   /evidence="ECO:0000269|PubMed:3888972"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   HELIX           58..61
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   TURN            108..111
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          112..118
FT                   /evidence="ECO:0007829|PDB:1BHU"
FT   STRAND          121..129
FT                   /evidence="ECO:0007829|PDB:1BHU"
SQ   SEQUENCE   131 AA;  13186 MW;  D204C23A57A67BD1 CRC64;
     MVRKRALGLA GSALTLVLGA VGFTAPAQAA PSCPAGSLCT YSGTGLSGAR TVIPASDMEK
     AGTDGVKLPA SARSFANGTH FTLRYGPARK VTCVRFPCYQ YATVGKVAPG AQLRSLPSPG
     ATVTVGQDLG D