ID   O85670_DICCH            Unreviewed;       120 AA.
AC   O85670;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   SubName: Full=Protease inhibitor {ECO:0000313|EMBL:AAC24002.1};
GN   Name=inh {ECO:0000313|EMBL:AAC24002.1};
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556 {ECO:0000313|EMBL:AAC24002.1};
RN   [1] {ECO:0000313|EMBL:AAC24002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EC16 {ECO:0000313|EMBL:AAC24002.1};
RX   PubMed=2211513;
RA   Dahler G.S., Barras F., Keen N.T.;
RT   "Cloning of genes encoding extracellular metalloproteases from Erwinia
RT   chrysanthemi EC16.";
RL   J. Bacteriol. 172:5803-5815(1990).
RN   [2] {ECO:0000313|EMBL:AAC24002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EC16 {ECO:0000313|EMBL:AAC24002.1};
RA   Bae K.H., Keen N.T., Byun S.M.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I38 family.
CC       {ECO:0000256|ARBA:ARBA00006813}.
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DR   EMBL; AF071511; AAC24002.1; -; Genomic_DNA.
DR   RefSeq; WP_081642155.1; NZ_CP128510.1.
DR   AlphaFoldDB; O85670; -.
DR   MEROPS; I38.003; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 2.40.128.10; -; 1.
DR   InterPro; IPR022815; Inh.
DR   InterPro; IPR021140; Inh/Omp19.
DR   InterPro; IPR016085; Protease_inh_B-barrel_dom.
DR   Pfam; PF02974; Inh; 1.
DR   PRINTS; PR01274; MPTASEINHBTR.
DR   SUPFAM; SSF50882; beta-Barrel protease inhibitors; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Metalloenzyme inhibitor {ECO:0000256|ARBA:ARBA00023215};
KW   Metalloprotease inhibitor {ECO:0000256|ARBA:ARBA00022608};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE-
KW   ProRule:PRU00303}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..120
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5050508891"
FT   CHAIN           20..120
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004160321"
FT   DOMAIN          25..118
FT                   /note="Alkaline proteinase inhibitor/ Outer membrane
FT                   lipoprotein Omp19"
FT                   /evidence="ECO:0000259|Pfam:PF02974"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   120 AA;  12869 MW;  EA97FE88BA92EA0B CRC64;
     MKQLIIATLL GVLSGGCMAS SLRLPSAAEL SGEWVLSGAE QRCDIRLKTD VLDSTTWTLS
     GDSACLNTLL PEVPAGWRPT PDGLTLTQAD GSAVAFFSRN RDHYEHKLAN GSVRILKKKA
//