ID   INH_DICCH               Reviewed;         120 AA.
AC   P18958; Q47301;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Proteinase inhibitor;
DE   Flags: Precursor;
GN   Name=inh;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-26.
RC   STRAIN=B374;
RX   PubMed=2654540; DOI=10.1111/j.1365-2958.1989.tb00106.x;
RA   Letoffe S., Delepelaire P., Wandersman C.;
RT   "Characterization of a protein inhibitor of extracellular proteases
RT   produced by Erwinia chrysanthemi.";
RL   Mol. Microbiol. 3:79-86(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=2184029; DOI=10.1002/j.1460-2075.1990.tb08252.x;
RA   Letoffe S., Delepelaire P., Wandersman C.;
RT   "Protease secretion by Erwinia chrysanthemi: the specific secretion
RT   functions are analogous to those of Escherichia coli alpha-haemolysin.";
RL   EMBO J. 9:1375-1382(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PROTEASE.
RC   STRAIN=B374;
RX   PubMed=7752231; DOI=10.1006/jmbi.1995.0249;
RA   Baumann U., Bauer M., Letoffe S., Delepelaire P., Wandersman C.;
RT   "Crystal structure of a complex between Serratia marcescens metallo-
RT   protease and an inhibitor from Erwinia chrysanthemi.";
RL   J. Mol. Biol. 248:653-661(1995).
CC   -!- FUNCTION: Inhibitor of the extracellular proteases A, B, and C of
CC       E.chrysanthemi and the S.marcescens 50 kDa extracellular protease. It
CC       forms a non-covalent bond with the proteases and may prevent
CC       autocatalytic cleavage of the proteases zymogen in the periplasm.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7752231}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I38 family.
CC       {ECO:0000305}.
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DR   EMBL; M60395; AAA63633.1; -; Genomic_DNA.
DR   EMBL; X53253; CAA37341.1; -; Genomic_DNA.
DR   EMBL; X14738; CAA32868.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S12524; S12524.
DR   PDB; 1SMP; X-ray; 2.30 A; I=20-120.
DR   PDBsum; 1SMP; -.
DR   AlphaFoldDB; P18958; -.
DR   SMR; P18958; -.
DR   MINT; P18958; -.
DR   MEROPS; I38.001; -.
DR   EvolutionaryTrace; P18958; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR022815; Inh.
DR   InterPro; IPR021140; Inh/Omp19.
DR   InterPro; IPR016085; Protease_inh_b-brl_dom.
DR   Pfam; PF02974; Inh; 1.
DR   PRINTS; PR01274; MPTASEINHBTR.
DR   SUPFAM; SSF50882; SSF50882; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Periplasm;
KW   Protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:2654540"
FT   CHAIN           20..120
FT                   /note="Proteinase inhibitor"
FT                   /id="PRO_0000026714"
FT   DISULFID        43..65
FT   HELIX           27..30
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          42..53
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   HELIX           63..69
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          93..100
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:1SMP"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:1SMP"
SQ   SEQUENCE   120 AA;  12909 MW;  F73BB59026E069D1 CRC64;
     MKQLIIATLL SALSGGCMAS SLRLPSAAEL SGQWVLSGAE QHCDIRLNTD VLDGTTWKLA
     GDTACLQKLL PEAPVGWRPT PDGLTLTQAD GSAVAFFSRN RDRYEHKLVD GSVRTLKKKA