ECOT_YERPY
ID ECOT_YERPY Reviewed; 169 AA.
AC B1JSA0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, 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=YPK_2851;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA69127.1; -; Genomic_DNA.
DR RefSeq; WP_002210815.1; NZ_CP009792.1.
DR PDB; 2Y6T; X-ray; 2.74 A; E/F/G/H=22-169.
DR PDBsum; 2Y6T; -.
DR AlphaFoldDB; B1JSA0; -.
DR SMR; B1JSA0; -.
DR MEROPS; I11.001; -.
DR EnsemblBacteria; ACA69127; ACA69127; YPK_2851.
DR GeneID; 66842315; -.
DR KEGG; ypy:YPK_2851; -.
DR PATRIC; fig|502800.11.peg.3566; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Periplasm; Protease inhibitor;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT CHAIN 22..169
FT /note="Ecotin"
FT /id="PRO_5000316227"
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"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2Y6T"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2Y6T"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2Y6T"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2Y6T"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:2Y6T"
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