ECOT_ECOLI
ID ECOT_ECOLI Reviewed; 162 AA.
AC P23827;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ecotin;
DE Flags: Precursor;
GN Name=eco; Synonyms=eti; OrderedLocusNames=b2209, JW2197;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-25 AND
RP 105-109.
RX PubMed=2007606; DOI=10.1016/s0021-9258(18)38162-6;
RA McGrath M.E., Hines W.M., Sakanari J.A., Fletterick R.J., Craik C.S.;
RT "The sequence and reactive site of ecotin. A general inhibitor of
RT pancreatic serine proteases from Escherichia coli.";
RL J. Biol. Chem. 266:6620-6625(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1879537; DOI=10.1016/0014-5793(91)80014-t;
RA Lee H.R., Seol J.H., Kim O.M., Lee C.S., Suh S.W., Hong Y.M., Tanaka K.,
RA Ichihara A., Ha D.B., Chung C.H.;
RT "Molecular cloning of the ecotin gene in Escherichia coli.";
RL FEBS Lett. 287:53-56(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 21-32.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8156987; DOI=10.1002/j.1460-2075.1994.tb06411.x;
RA McGrath M.E., Erpel T., Bystroff C., Fletterick R.J.;
RT "Macromolecular chelation as an improved mechanism of protease inhibition:
RT structure of the ecotin-trypsin complex.";
RL EMBO J. 13:1502-1507(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS).
RX PubMed=8931142; DOI=10.1002/pro.5560051110;
RA Shin D.H.A., Song H.K., Seong I.S., Lee C.S., Chung C.H., Suh S.W.;
RT "Crystal structure analyses of uncomplexed ecotin in two crystal forms:
RT implications for its function and stability.";
RL Protein Sci. 5:2236-2247(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH UCA COLLAGENASE.
RX PubMed=9154920; DOI=10.1021/bi9617522;
RA Perona J.J., Tsu C.A., Craik C.S., Fletterick R.J.;
RT "Crystal structure of an ecotin-collagenase complex suggests a model for
RT recognition and cleavage of the collagen triple helix.";
RL Biochemistry 36:5381-5392(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10843853; DOI=10.1006/jmbi.2000.3812;
RA Gillmor S.A., Takeuchi T., Yang S.Q., Craik C.S., Fletterick R.J.;
RT "Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor
RT of serine proteases.";
RL J. Mol. Biol. 299:993-1003(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ARG-104.
RX PubMed=11513582; DOI=10.1021/bi010712h;
RA Wang S.X., Esmon C.T., Fletterick R.J.;
RT "Crystal structure of thrombin-ecotin reveals conformational changes and
RT extended interactions.";
RL Biochemistry 40:10038-10046(2001).
RN [14]
RP REVIEW.
RX PubMed=7757004; DOI=10.1002/pro.5560040201;
RA McGrath M.E., Gillmor S.A., Fletterick R.J.;
RT "Ecotin: lessons on survival in a protease-filled world.";
RL Protein Sci. 4:141-148(1995).
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. The strength of inhibition does not appear
CC to be correlated with a particular protease specificity.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P23827; P03951: F11; Xeno; NbExp=3; IntAct=EBI-1029159, EBI-1041019;
CC P23827; P48740-2: MASP1; Xeno; NbExp=3; IntAct=EBI-1029159, EBI-26435098;
CC P23827; P00763: Prss2; Xeno; NbExp=2; IntAct=EBI-1029159, EBI-1029166;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the protease inhibitor I11 (ecotin) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60876; AAA23719.1; -; Genomic_DNA.
DR EMBL; X61951; CAA43954.1; -; Genomic_DNA.
DR EMBL; U00008; AAA16410.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75269.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15992.1; -; Genomic_DNA.
DR PIR; A38742; A38742.
DR RefSeq; NP_416713.1; NC_000913.3.
DR RefSeq; WP_000849209.1; NZ_SSZK01000027.1.
DR PDB; 1AZZ; X-ray; 2.30 A; C/D=21-162.
DR PDB; 1ECY; X-ray; 2.19 A; A=21-162.
DR PDB; 1ECZ; X-ray; 2.68 A; A/B=21-162.
DR PDB; 1EZS; X-ray; 2.30 A; A/B=21-162.
DR PDB; 1EZU; X-ray; 2.40 A; A/B=21-162.
DR PDB; 1FI8; X-ray; 2.20 A; C/E=21-109, D/F=105-162.
DR PDB; 1ID5; X-ray; 2.50 A; I=21-162.
DR PDB; 1IFG; X-ray; 2.00 A; A=26-162.
DR PDB; 1N8O; X-ray; 2.00 A; E=21-162.
DR PDB; 1P0S; X-ray; 2.80 A; E=21-162.
DR PDB; 1SLU; X-ray; 1.80 A; A=21-162.
DR PDB; 1SLV; X-ray; 2.30 A; A=21-162.
DR PDB; 1SLW; X-ray; 2.00 A; A=21-162.
DR PDB; 1SLX; X-ray; 2.20 A; A=21-162.
DR PDB; 1XX9; X-ray; 2.20 A; C/D=21-162.
DR PDB; 1XXD; X-ray; 2.91 A; C/D=21-162.
DR PDB; 1XXF; X-ray; 2.60 A; C/D=21-162.
DR PDB; 4IW4; X-ray; 3.20 A; C/D=21-162.
DR PDB; 4NIY; X-ray; 2.84 A; E/F/G/H=21-162.
DR PDB; 7CBK; X-ray; 2.70 A; A/C=1-162.
DR PDBsum; 1AZZ; -.
DR PDBsum; 1ECY; -.
DR PDBsum; 1ECZ; -.
DR PDBsum; 1EZS; -.
DR PDBsum; 1EZU; -.
DR PDBsum; 1FI8; -.
DR PDBsum; 1ID5; -.
DR PDBsum; 1IFG; -.
DR PDBsum; 1N8O; -.
DR PDBsum; 1P0S; -.
DR PDBsum; 1SLU; -.
DR PDBsum; 1SLV; -.
DR PDBsum; 1SLW; -.
DR PDBsum; 1SLX; -.
DR PDBsum; 1XX9; -.
DR PDBsum; 1XXD; -.
DR PDBsum; 1XXF; -.
DR PDBsum; 4IW4; -.
DR PDBsum; 4NIY; -.
DR PDBsum; 7CBK; -.
DR AlphaFoldDB; P23827; -.
DR PCDDB; P23827; -.
DR SMR; P23827; -.
DR BioGRID; 4262218; 13.
DR BioGRID; 851041; 1.
DR IntAct; P23827; 8.
DR MINT; P23827; -.
DR STRING; 511145.b2209; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR MEROPS; I11.001; -.
DR jPOST; P23827; -.
DR PaxDb; P23827; -.
DR PRIDE; P23827; -.
DR EnsemblBacteria; AAC75269; AAC75269; b2209.
DR EnsemblBacteria; BAA15992; BAA15992; BAA15992.
DR GeneID; 946700; -.
DR KEGG; ecj:JW2197; -.
DR KEGG; eco:b2209; -.
DR PATRIC; fig|1411691.4.peg.26; -.
DR EchoBASE; EB0251; -.
DR eggNOG; COG4574; Bacteria.
DR HOGENOM; CLU_111565_0_0_6; -.
DR InParanoid; P23827; -.
DR OMA; PKAEKGM; -.
DR PhylomeDB; P23827; -.
DR BioCyc; EcoCyc:EG10255-MON; -.
DR EvolutionaryTrace; P23827; -.
DR PRO; PR:P23827; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2007606,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 21..162
FT /note="Ecotin"
FT /id="PRO_0000007423"
FT SITE 104..105
FT /note="Reactive bond"
FT DISULFID 70..107
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1IFG"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1SLU"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 56..68
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1XXD"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1SLU"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1IFG"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1SLU"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1EZS"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1SLU"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1SLU"
SQ SEQUENCE 162 AA; 18192 MW; E965383177B92ECD CRC64;
MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ EDESTLKVEL
LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY
LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAV VR
