ID   ECOT_YERPN              Reviewed;         169 AA.
AC   Q1CFY7; C4GWC9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=YPN_2766;
GN   ORFNames=YP516_3126;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000305; ABG19093.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000017; EEO75229.1; -; Genomic_DNA.
DR   RefSeq; WP_002210815.1; NZ_ACNQ01000017.1.
DR   AlphaFoldDB; Q1CFY7; -.
DR   SMR; Q1CFY7; -.
DR   MEROPS; I11.001; -.
DR   EnsemblBacteria; ABG19093; ABG19093; YPN_2766.
DR   GeneID; 66842315; -.
DR   KEGG; ypn:YPN_2766; -.
DR   HOGENOM; CLU_111565_0_0_6; -.
DR   OMA; PKAEKGM; -.
DR   Proteomes; UP000008936; Chromosome.
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_5000115497"
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