ID   ECOT_ECOLC              Reviewed;         162 AA.
AC   B1IY63;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=EcolC_1441;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: General inhibitor of pancreatic serine proteases: inhibits
CC       chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a
CC       variety of other proteases. {ECO:0000255|HAMAP-Rule:MF_00706}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00706}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00706}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I11 (ecotin) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00706}.
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DR   EMBL; CP000946; ACA77104.1; -; Genomic_DNA.
DR   RefSeq; WP_000849209.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IY63; -.
DR   SMR; B1IY63; -.
DR   MEROPS; I11.001; -.
DR   KEGG; ecl:EcolC_1441; -.
DR   HOGENOM; CLU_111565_0_0_6; -.
DR   OMA; PKAEKGM; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00242; Ecotin; 1.
DR   Gene3D; 4.10.1230.10; -; 1.
DR   HAMAP; MF_00706; Ecotin; 1.
DR   InterPro; IPR027438; Ecotin_C.
DR   InterPro; IPR036198; Ecotin_sf.
DR   InterPro; IPR005658; Prot_inh_ecotin.
DR   InterPro; IPR023084; Prot_inh_ecotin_gammaproteobac.
DR   PANTHER; PTHR35890; PTHR35890; 1.
DR   Pfam; PF03974; Ecotin; 1.
DR   PIRSF; PIRSF006865; Prot_inh_ecotin; 1.
DR   SUPFAM; SSF49772; SSF49772; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Periplasm; Protease inhibitor; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   CHAIN           21..162
FT                   /note="Ecotin"
FT                   /id="PRO_5000314249"
FT   SITE            104..105
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   DISULFID        70..107
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ   SEQUENCE   162 AA;  18192 MW;  E965383177B92ECD CRC64;
     MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ EDESTLKVEL
     LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY
     LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAV VR