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Protein

Ecotin

Gene

eco

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei104 – 1052Reactive bond

GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: EcoCyc

GO - Biological processi

  • negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Enzyme and pathway databases

BioCyciEcoCyc:EG10255-MONOMER.
ECOL316407:JW2197-MONOMER.

Protein family/group databases

MEROPSiI11.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ecotin
Gene namesi
Name:eco
Synonyms:eti
Ordered Locus Names:b2209, JW2197
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10255. eco.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 162142EcotinPRO_0000007423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 107

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP23827.
PRIDEiP23827.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
F11P039513EBI-1029159,EBI-1041019From a different organism.
Prss2P007632EBI-1029159,EBI-1029166From a different organism.

Protein-protein interaction databases

IntActiP23827. 6 interactions.
MINTiMINT-276115.
STRINGi511145.b2209.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 293Combined sources
Beta strandi40 – 456Combined sources
Helixi53 – 553Combined sources
Beta strandi56 – 6813Combined sources
Beta strandi70 – 723Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 836Combined sources
Turni85 – 873Combined sources
Beta strandi90 – 956Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi113 – 1197Combined sources
Helixi122 – 1254Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi144 – 1518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23827.
SMRiP23827. Positions 21-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23827.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4574.
HOGENOMiHOG000263245.
InParanoidiP23827.
KOiK08276.
OMAiPKAEKGM.
OrthoDBiEOG6P0711.
PhylomeDBiP23827.

Family and domain databases

Gene3Di2.60.40.550. 1 hit.
4.10.1230.10. 1 hit.
HAMAPiMF_00706. Ecotin.
InterProiIPR027438. Ecotin_C.
IPR005658. Prot_inh_ecotin.
IPR023189. Prot_inh_ecotin_dom.
IPR023084. Prot_inh_ecotin_gammaproteobac.
[Graphical view]
PfamiPF03974. Ecotin. 1 hit.
[Graphical view]
PIRSFiPIRSF006865. Prot_inh_ecotin. 1 hit.
SUPFAMiSSF49772. SSF49772. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ
60 70 80 90 100
EDESTLKVEL LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP
110 120 130 140 150
VSTMMACPDG KKEKKFVTAY LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW
160
KAEEKIDNAV VR
Length:162
Mass (Da):18,192
Last modified:November 1, 1991 - v1
Checksum:iE965383177B92ECD
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA38742.
RefSeqiNP_416713.1. NC_000913.3.
WP_000849209.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75269; AAC75269; b2209.
BAA15992; BAA15992; BAA15992.
GeneIDi946700.
KEGGieco:b2209.
PATRICi32119777. VBIEscCol129921_2298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA38742.
RefSeqiNP_416713.1. NC_000913.3.
WP_000849209.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23827.
SMRiP23827. Positions 21-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23827. 6 interactions.
MINTiMINT-276115.
STRINGi511145.b2209.

Protein family/group databases

MEROPSiI11.001.

Proteomic databases

PaxDbiP23827.
PRIDEiP23827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75269; AAC75269; b2209.
BAA15992; BAA15992; BAA15992.
GeneIDi946700.
KEGGieco:b2209.
PATRICi32119777. VBIEscCol129921_2298.

Organism-specific databases

EchoBASEiEB0251.
EcoGeneiEG10255. eco.

Phylogenomic databases

eggNOGiCOG4574.
HOGENOMiHOG000263245.
InParanoidiP23827.
KOiK08276.
OMAiPKAEKGM.
OrthoDBiEOG6P0711.
PhylomeDBiP23827.

Enzyme and pathway databases

BioCyciEcoCyc:EG10255-MONOMER.
ECOL316407:JW2197-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP23827.
PROiP23827.

Family and domain databases

Gene3Di2.60.40.550. 1 hit.
4.10.1230.10. 1 hit.
HAMAPiMF_00706. Ecotin.
InterProiIPR027438. Ecotin_C.
IPR005658. Prot_inh_ecotin.
IPR023189. Prot_inh_ecotin_dom.
IPR023084. Prot_inh_ecotin_gammaproteobac.
[Graphical view]
PfamiPF03974. Ecotin. 1 hit.
[Graphical view]
PIRSFiPIRSF006865. Prot_inh_ecotin. 1 hit.
SUPFAMiSSF49772. SSF49772. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. 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.

Entry informationi

Entry nameiECOT_ECOLI
AccessioniPrimary (citable) accession number: P23827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 22, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.