ECOT_SHIFL
ID ECOT_SHIFL Reviewed; 162 AA.
AC Q821B1;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-SEP-2003, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE Flags: Precursor;
GN Name=eco {ECO:0000255|HAMAP-Rule:MF_00706};
GN OrderedLocusNames=SF2293, S2423;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN43812.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17629.1; -; Genomic_DNA.
DR RefSeq; NP_708105.2; NC_004337.2.
DR RefSeq; WP_005046814.1; NZ_WPGW01000022.1.
DR AlphaFoldDB; Q821B1; -.
DR SMR; Q821B1; -.
DR STRING; 198214.SF2293; -.
DR MEROPS; I11.001; -.
DR EnsemblBacteria; AAN43812; AAN43812; SF2293.
DR EnsemblBacteria; AAP17629; AAP17629; S2423.
DR GeneID; 1025479; -.
DR GeneID; 58388750; -.
DR KEGG; sfl:SF2293; -.
DR KEGG; sfx:S2423; -.
DR PATRIC; fig|198214.7.peg.2744; -.
DR HOGENOM; CLU_111565_0_0_6; -.
DR OMA; PKAEKGM; -.
DR OrthoDB; 1603172at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT CHAIN 21..162
FT /note="Ecotin"
FT /id="PRO_0000007433"
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; 18226 MW; E97650F373CC5BB9 CRC64;
MKTILPEVLF AAFATTSAWA AESVQPLEKI APYPQAETGM KRQVIQLTPQ EDESTLKVEL
LIGQTLEVDC NLHRLGGKLE SKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY
LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAE VR