ECOT_YERPG
ID ECOT_YERPG Reviewed; 169 AA.
AC A9R289;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE Flags: Precursor;
GN Name=eco {ECO:0000255|HAMAP-Rule:MF_00706};
GN OrderedLocusNames=YpAngola_A1316;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX88280.1; -; Genomic_DNA.
DR RefSeq; WP_002210815.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R289; -.
DR SMR; A9R289; -.
DR MEROPS; I11.001; -.
DR GeneID; 66842315; -.
DR KEGG; ypg:YpAngola_A1316; -.
DR PATRIC; fig|349746.12.peg.2282; -.
DR OMA; PKAEKGM; -.
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 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; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT CHAIN 22..169
FT /note="Ecotin"
FT /id="PRO_1000132367"
FT SITE 110..111
FT /note="Reactive bond"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT DISULFID 76..113
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ SEQUENCE 169 AA; 18871 MW; EFD86EFBB7F6FF16 CRC64;
MKKCSIILAS VLLATSINAI ADTPTPLNQQ QPLEKIAPYP QAEKGMSRQV IFLEPQKDES
RFKVELLIGK TLNVDCNRHM LGGNLETRTL SGWGFDYLVM DKISQPASTM MACPEDSKPQ
VKFVTANLGD AAMQRYNSRL PIVVYVPQGV EVKYRIWEAG EDIRSAQVK