ECOT_SALTI
ID ECOT_SALTI Reviewed; 164 AA.
AC Q8Z568;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE Flags: Precursor;
GN Name=eco {ECO:0000255|HAMAP-Rule:MF_00706};
GN OrderedLocusNames=STY2488, t0602;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07494.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68307.1; -; Genomic_DNA.
DR RefSeq; NP_456807.1; NC_003198.1.
DR RefSeq; WP_001764187.1; NZ_WSUR01000051.1.
DR AlphaFoldDB; Q8Z568; -.
DR SMR; Q8Z568; -.
DR STRING; 220341.16503489; -.
DR MEROPS; I11.001; -.
DR EnsemblBacteria; AAO68307; AAO68307; t0602.
DR KEGG; stt:t0602; -.
DR KEGG; sty:STY2488; -.
DR PATRIC; fig|220341.7.peg.2520; -.
DR eggNOG; COG4574; Bacteria.
DR HOGENOM; CLU_111565_0_0_6; -.
DR OMA; PKAEKGM; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..164
FT /note="Ecotin"
FT /id="PRO_0000007430"
FT SITE 106..107
FT /note="Reactive bond"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT DISULFID 72..109
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ SEQUENCE 164 AA; 18232 MW; F7E78BD0D71080E3 CRC64;
MKMFVPAVVF AALASASAWA NNGDTAQPLE KIAPYPQAEK GMKRQVITLT PQQDESTLKV
ELLIGQTLNV DCNQHRLGGT LETKTLEGWG YDYYVFDNVT SPVSTMMACP EGKKEQKFVT
AWLGEDGMLR YNSKLPIVVY TPANVDVKYR IWKADANVQN AIAR