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P23827 (ECOT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ecotin
Gene names
Name:eco
Synonyms:eti
Ordered Locus Names:b2209, JW2197
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity. HAMAP-Rule MF_00706

Subunit structure

Homodimer.

Subcellular location

Periplasm HAMAP-Rule MF_00706.

Sequence similarities

Belongs to the protease inhibitor I11 (ecotin) family. [View classification]

Sequence caution

The sequence AAA16410.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

F11P039513EBI-1029159,EBI-1041019From a different organism.
Prss2P007632EBI-1029159,EBI-1029166From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1 Ref.7
Chain21 – 162142Ecotin HAMAP-Rule MF_00706
PRO_0000007423

Sites

Site104 – 1052Reactive bond

Amino acid modifications

Disulfide bond70 ↔ 107 HAMAP-Rule MF_00706

Secondary structure

................................ 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23827 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: E965383177B92ECD

FASTA16218,192
        10         20         30         40         50         60 
MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ EDESTLKVEL 

        70         80         90        100        110        120 
LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY 

       130        140        150        160 
LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAV VR 

« Hide

References

« Hide 'large scale' references
[1]"The sequence and reactive site of ecotin. A general inhibitor of pancreatic serine proteases from Escherichia coli."
McGrath M.E., Hines W.M., Sakanari J.A., Fletterick R.J., Craik C.S.
J. Biol. Chem. 266:6620-6625(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-25 AND 105-109.
[2]"Molecular cloning of the ecotin gene in Escherichia coli."
Lee H.R., Seol J.H., Kim O.M., Lee C.S., Suh S.W., Hong Y.M., Tanaka K., Ichihara A., Ha D.B., Chung C.H.
FEBS Lett. 287:53-56(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Automated multiplex sequencing of the E.coli genome."
Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / BHB2600.
[4]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-32.
Strain: K12 / EMG2.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex."
McGrath M.E., Erpel T., Bystroff C., Fletterick R.J.
EMBO J. 13:1502-1507(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[10]"Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability."
Shin D.H.A., Song H.K., Seong I.S., Lee C.S., Chung C.H., Suh S.W.
Protein Sci. 5:2236-2247(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS).
[11]"Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix."
Perona J.J., Tsu C.A., Craik C.S., Fletterick R.J.
Biochemistry 36:5381-5392(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH UCA COLLAGENASE.
[12]"Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases."
Gillmor S.A., Takeuchi T., Yang S.Q., Craik C.S., Fletterick R.J.
J. Mol. Biol. 299:993-1003(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[13]"Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions."
Wang S.X., Esmon C.T., Fletterick R.J.
Biochemistry 40:10038-10046(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ARG-104.
[14]"Ecotin: lessons on survival in a protease-filled world."
McGrath M.E., Gillmor S.A., Fletterick R.J.
Protein Sci. 4:141-148(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60876 Genomic DNA. Translation: AAA23719.1.
X61951 Genomic DNA. Translation: CAA43954.1.
U00008 Genomic DNA. Translation: AAA16410.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75269.1.
AP009048 Genomic DNA. Translation: BAA15992.1.
PIRA38742.
RefSeqNP_416713.1. NC_000913.3.
YP_490447.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZZX-ray2.30C/D21-162[»]
1ECYX-ray2.19A21-162[»]
1ECZX-ray2.68A/B21-162[»]
1EZSX-ray2.30A/B21-162[»]
1EZUX-ray2.40A/B21-162[»]
1FI8X-ray2.20C/E21-109[»]
D/F105-162[»]
1ID5X-ray2.50I21-162[»]
1IFGX-ray2.00A26-162[»]
1N8OX-ray2.00E21-162[»]
1P0SX-ray2.80E21-162[»]
1SLUX-ray1.80A21-162[»]
1SLVX-ray2.30A21-162[»]
1SLWX-ray2.00A21-162[»]
1SLXX-ray2.20A21-162[»]
1XX9X-ray2.20C/D21-162[»]
1XXDX-ray2.91C/D21-162[»]
1XXFX-ray2.60C/D21-162[»]
4IW4X-ray3.20C/D21-162[»]
4NIYX-ray2.84E/F/G/H21-162[»]
ProteinModelPortalP23827.
SMRP23827. Positions 21-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP23827. 6 interactions.
MINTMINT-276115.
STRING511145.b2209.

Protein family/group databases

MEROPSI11.001.

Proteomic databases

PaxDbP23827.
PRIDEP23827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75269; AAC75269; b2209.
BAA15992; BAA15992; BAA15992.
GeneID12933224.
946700.
KEGGecj:Y75_p2170.
eco:b2209.
PATRIC32119777. VBIEscCol129921_2298.

Organism-specific databases

EchoBASEEB0251.
EcoGeneEG10255. eco.

Phylogenomic databases

eggNOGCOG4574.
HOGENOMHOG000263245.
KOK08276.
OMARFRTWKV.
OrthoDBEOG6P0711.
PhylomeDBP23827.

Enzyme and pathway databases

BioCycEcoCyc:EG10255-MONOMER.
ECOL316407:JW2197-MONOMER.

Gene expression databases

GenevestigatorP23827.

Family and domain databases

Gene3D2.60.40.550. 1 hit.
4.10.1230.10. 1 hit.
HAMAPMF_00706. Ecotin.
InterProIPR027438. Ecotin_C.
IPR005658. Prot_inh_ecotin.
IPR023189. Prot_inh_ecotin_dom.
IPR023084. Prot_inh_ecotin_gammaproteobac.
[Graphical view]
PfamPF03974. Ecotin. 1 hit.
[Graphical view]
PIRSFPIRSF006865. Prot_inh_ecotin. 1 hit.
SUPFAMSSF49772. SSF49772. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP23827.
PROP23827.

Entry information

Entry nameECOT_ECOLI
AccessionPrimary (citable) accession number: P23827
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene