ID   ECOT_PSEP1              Reviewed;         159 AA.
AC   A5W3S6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=Pput_2652;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ78786.1; -; Genomic_DNA.
DR   RefSeq; WP_012052429.1; NC_009512.1.
DR   AlphaFoldDB; A5W3S6; -.
DR   SMR; A5W3S6; -.
DR   STRING; 351746.Pput_2652; -.
DR   MEROPS; I11.003; -.
DR   EnsemblBacteria; ABQ78786; ABQ78786; Pput_2652.
DR   KEGG; ppf:Pput_2652; -.
DR   eggNOG; COG4574; Bacteria.
DR   HOGENOM; CLU_111565_0_0_6; -.
DR   OMA; PKAEKGM; -.
DR   OrthoDB; 1603172at2; -.
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..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   CHAIN           23..159
FT                   /note="Ecotin"
FT                   /id="PRO_5000252064"
FT   SITE            102..103
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   DISULFID        68..105
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ   SEQUENCE   159 AA;  17401 MW;  C79B2387EA24C44F CRC64;
     MRPTPMTAIL ALSLAAAAPA MAASLKDIAP YPEAEKGFTR QVIHLPAQAD ESAYKLEILA
     GKTLQVDCNR QRLGGNLEAR TLEGWGYNYY RLDNVSGPAS TLMACPDGKK TEAFVPVVGD
     GFLLRYNSKL PVVVYVPKDV EVRYRVWSAS QDVQKAKVE