ID   ECOT_SHEON              Reviewed;         183 AA.
AC   Q8EEQ7;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=SO_2312;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- FUNCTION: General inhibitor of family S1 serine proteases.
CC       {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; AE014299; AAN55351.1; -; Genomic_DNA.
DR   RefSeq; NP_717907.1; NC_004347.2.
DR   RefSeq; WP_011072312.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EEQ7; -.
DR   SMR; Q8EEQ7; -.
DR   MEROPS; I11.001; -.
DR   PaxDb; Q8EEQ7; -.
DR   KEGG; son:SO_2312; -.
DR   PATRIC; fig|211586.12.peg.2227; -.
DR   eggNOG; COG4574; Bacteria.
DR   HOGENOM; CLU_111565_0_1_6; -.
DR   OMA; PKAEKGM; -.
DR   OrthoDB; 1603172at2; -.
DR   PhylomeDB; Q8EEQ7; -.
DR   BioCyc; SONE211586:G1GMP-2114-MON; -.
DR   Proteomes; UP000008186; 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   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; Reference proteome;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   CHAIN           26..183
FT                   /note="Ecotin"
FT                   /id="PRO_0000007432"
FT   SITE            129..130
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   DISULFID        95..132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ   SEQUENCE   183 AA;  20580 MW;  DCA664F4C0E636C3 CRC64;
     MKLPQLCHLA AVPLAFTLLS FNASAVSPPH PTGLDAPMIS VSSMNANNYA PVETVKMFPA
     PKKGMVQHIL TLPKLENETD YMVEIQIGQT QLVDCNKHGL NGQLKELTVE GWGYNYYQVD
     EISEGPSTMM ACFELAKKEA FVQIPDELTL RYDSRLPKVF YLPEGAELRF RTWKADSTYQ
     YSK