ID   ECOT_YERPB              Reviewed;         169 AA.
AC   B2K9A0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-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=YPTS_1338;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-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; CP001048; ACC88313.1; -; Genomic_DNA.
DR   RefSeq; WP_002210815.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K9A0; -.
DR   SMR; B2K9A0; -.
DR   MEROPS; I11.001; -.
DR   GeneID; 66842315; -.
DR   KEGG; ypb:YPTS_1338; -.
DR   PATRIC; fig|502801.10.peg.691; -.
DR   OMA; PKAEKGM; -.
DR   BioCyc; YPSE502801:YPTS_RS06875-MON; -.
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   HAMAP; MF_00706; Ecotin; 1.
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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   CHAIN           22..169
FT                   /note="Ecotin"
FT                   /id="PRO_5000345931"
FT   SITE            110..111
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   DISULFID        76..113
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ   SEQUENCE   169 AA;  18871 MW;  EFD86EFBB7F6FF16 CRC64;
     MKKCSIILAS VLLATSINAI ADTPTPLNQQ QPLEKIAPYP QAEKGMSRQV IFLEPQKDES
     RFKVELLIGK TLNVDCNRHM LGGNLETRTL SGWGFDYLVM DKISQPASTM MACPEDSKPQ
     VKFVTANLGD AAMQRYNSRL PIVVYVPQGV EVKYRIWEAG EDIRSAQVK