ECOT_SHISS
ID ECOT_SHISS Reviewed; 162 AA.
AC Q3YZZ8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE Flags: Precursor;
GN Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=SSON_2267;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ88914.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZZ8; -.
DR SMR; Q3YZZ8; -.
DR MEROPS; I11.001; -.
DR EnsemblBacteria; AAZ88914; AAZ88914; SSON_2267.
DR KEGG; ssn:SSON_2267; -.
DR HOGENOM; CLU_111565_0_0_6; -.
DR OMA; PKAEKGM; -.
DR Proteomes; UP000002529; 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..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT CHAIN 21..162
FT /note="Ecotin"
FT /id="PRO_0000225651"
FT SITE 104..105
FT /note="Reactive bond"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT DISULFID 70..107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ SEQUENCE 162 AA; 18180 MW; E1C7A9886747CE23 CRC64;
MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ EDESTLKVEL
LTGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY
LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAV VR