ID   ECOT_PROMM              Reviewed;         177 AA.
AC   P59839;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-SEP-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE   Flags: Precursor;
GN   Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=PMT_2221;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE22395.1; -; Genomic_DNA.
DR   RefSeq; WP_011131585.1; NC_005071.1.
DR   AlphaFoldDB; P59839; -.
DR   SMR; P59839; -.
DR   STRING; 74547.PMT_2221; -.
DR   EnsemblBacteria; CAE22395; CAE22395; PMT_2221.
DR   KEGG; pmt:PMT_2221; -.
DR   eggNOG; COG4574; Bacteria.
DR   HOGENOM; CLU_1516607_0_0_3; -.
DR   OMA; GQTKMVD; -.
DR   OrthoDB; 1603172at2; -.
DR   Proteomes; UP000001423; 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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   CHAIN           24..177
FT                   /note="Ecotin"
FT                   /id="PRO_0000007426"
FT   SITE            119..120
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT   DISULFID        83..122
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ   SEQUENCE   177 AA;  20070 MW;  50858ADAA434BD7C CRC64;
     MQASIQNRIF FGLVVLWSTT VLEPLRAIPR MDLNDYPQPI AGHQRWVIQL PGLLAKSSDP
     GLSTNAVDWR VQLIVGRTIQ LVCNQYHLAG QGLRMERFQG AEQRMLYSVA GAVKVMSTRM
     VCPPDEPKRE SFLVLGSKPY LVPYNASFPI VVDVPDGLEV RWRLWKAEIT QREAIKL