ID   ECOT_PSEPG              Reviewed;         159 AA.
AC   B0KU25;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=PputGB1_2794;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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; CP000926; ABY98688.1; -; Genomic_DNA.
DR   RefSeq; WP_012272426.1; NC_010322.1.
DR   AlphaFoldDB; B0KU25; -.
DR   SMR; B0KU25; -.
DR   STRING; 76869.PputGB1_2794; -.
DR   MEROPS; I11.003; -.
DR   EnsemblBacteria; ABY98688; ABY98688; PputGB1_2794.
DR   KEGG; ppg:PputGB1_2794; -.
DR   eggNOG; COG4574; Bacteria.
DR   HOGENOM; CLU_111565_0_0_6; -.
DR   OMA; PKAEKGM; -.
DR   Proteomes; UP000002157; 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; 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_5000305799"
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;  17432 MW;  5FEC63DBF2E68A3A CRC64;
     MRPTPMTAIL ALTLAAAAPA MAASLKDVAP YPEAEKGFTR QVIHLPAQAD ESAYKLEILA
     GKTLKVDCNR QRLGGSLEER TLEGWGYNYY RLDKVSGPAS TLMACPDGKK TEAFVPVVGD
     GFLLRYNSKL PVVVYVPKDV EVRYRVWSAS QDVQKANVE