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Database: UniProt
Entry: P23827
LinkDB: P23827
Original site: P23827 
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   10-APR-2019, entry version 161.
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;
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.,
RA   Tanaka K., 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.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 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
RT   in the 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.,
RA   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;
RA   McGrath M.E., Erpel T., Bystroff C., Fletterick R.J.;
RT   "Macromolecular chelation as an improved mechanism of protease
RT   inhibition: 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
RT   forms: 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
RT   for 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
RT   inhibitor 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
RT   and 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:
CC       inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as
CC       well as a variety of other proteases. The strength of inhibition
CC       does not appear to be correlated with a particular protease
CC       specificity.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P03951:F11 (xeno); NbExp=3; IntAct=EBI-1029159, EBI-1041019;
CC       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};
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_LN832404.1.
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   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   ProteinModelPortal; P23827; -.
DR   SMR; P23827; -.
DR   BioGrid; 4262218; 13.
DR   IntAct; P23827; 6.
DR   MINT; P23827; -.
DR   STRING; 511145.b2209; -.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   MEROPS; I11.001; -.
DR   EPD; P23827; -.
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   EcoGene; EG10255; eco.
DR   eggNOG; ENOG4108QSZ; Bacteria.
DR   eggNOG; COG4574; LUCA.
DR   HOGENOM; HOG000263245; -.
DR   InParanoid; P23827; -.
DR   KO; K08276; -.
DR   PhylomeDB; P23827; -.
DR   BioCyc; EcoCyc:EG10255-MONOMER; -.
DR   BioCyc; ECOL316407:JW2197-MONOMER; -.
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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Periplasm; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL        1     20       {ECO:0000269|PubMed:2007606,
FT                                ECO:0000269|PubMed:9298646}.
FT   CHAIN        21    162       Ecotin.
FT                                /FTId=PRO_0000007423.
FT   SITE        104    105       Reactive bond.
FT   DISULFID     70    107
FT   HELIX        27     29       {ECO:0000244|PDB:1IFG}.
FT   STRAND       40     45       {ECO:0000244|PDB:1SLU}.
FT   HELIX        53     55       {ECO:0000244|PDB:1SLU}.
FT   STRAND       56     68       {ECO:0000244|PDB:1SLU}.
FT   STRAND       70     72       {ECO:0000244|PDB:1XXD}.
FT   STRAND       73     75       {ECO:0000244|PDB:1SLU}.
FT   STRAND       78     83       {ECO:0000244|PDB:1SLU}.
FT   TURN         85     87       {ECO:0000244|PDB:1SLU}.
FT   STRAND       90     95       {ECO:0000244|PDB:1SLU}.
FT   STRAND      101    103       {ECO:0000244|PDB:1SLU}.
FT   STRAND      108    110       {ECO:0000244|PDB:1IFG}.
FT   STRAND      113    119       {ECO:0000244|PDB:1SLU}.
FT   HELIX       122    125       {ECO:0000244|PDB:1SLU}.
FT   STRAND      126    128       {ECO:0000244|PDB:1SLU}.
FT   STRAND      131    133       {ECO:0000244|PDB:1EZS}.
FT   STRAND      135    140       {ECO:0000244|PDB:1SLU}.
FT   STRAND      144    151       {ECO:0000244|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
//
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