ID   ECOT_SALTY              Reviewed;         164 AA.
AC   Q8ZNH4;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=STM2262;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL21164.1; -; Genomic_DNA.
DR   RefSeq; NP_461205.1; NC_003197.2.
DR   RefSeq; WP_000781589.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZNH4; -.
DR   SMR; Q8ZNH4; -.
DR   STRING; 99287.STM2262; -.
DR   MEROPS; I11.001; -.
DR   PaxDb; Q8ZNH4; -.
DR   EnsemblBacteria; AAL21164; AAL21164; STM2262.
DR   GeneID; 1253784; -.
DR   KEGG; stm:STM2262; -.
DR   PATRIC; fig|99287.12.peg.2396; -.
DR   HOGENOM; CLU_111565_0_0_6; -.
DR   OMA; PKAEKGM; -.
DR   PhylomeDB; Q8ZNH4; -.
DR   BioCyc; SENT99287:STM2262-MON; -.
DR   Proteomes; UP000001014; 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   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; Reference proteome;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   CHAIN           21..164
FT                   /note="Ecotin"
FT                   /id="PRO_0000007431"
FT   SITE            106..107
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   DISULFID        72..109
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ   SEQUENCE   164 AA;  18218 MW;  F7E79940D71080E3 CRC64;
     MKMFVPAVVF AALASASAWA NNGDTAQPLE KIAPYPQAEK GMKRQVITLT PQQDESTLKV
     ELLIGQTLNV DCNQHRLGGT LETKTLEGWG YDYYVFDNVT SPVSTMMACP EGKKEQKFVT
     AWLGEDGMLR YNSKLPIVVY TPANVDVKYR IWKADANVQN AVAR