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P23827

- ECOT_ECOLI

UniProt

P23827 - ECOT_ECOLI

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Protein
Ecotin
Gene
eco, eti, b2209, JW2197
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation

Sites

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

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. serine-type endopeptidase inhibitor activity Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10255. eco.

Subcellular locationi

Periplasm UniRule annotation

GO - Cellular componenti

  1. 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 Publications
Add
BLAST
Chaini21 – 162142EcotinUniRule annotation
PRO_0000007423Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP23827.
PRIDEiP23827.

Expressioni

Gene expression databases

GenevestigatoriP23827.

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP23827.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4574.
HOGENOMiHOG000263245.
KOiK08276.
OMAiRFRTWKV.
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

MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ    50
EDESTLKVEL LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP 100
VSTMMACPDG KKEKKFVTAY LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW 150
KAEEKIDNAV VR 162
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_490447.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75269; AAC75269; b2209.
BAA15992; BAA15992; BAA15992.
GeneIDi12933224.
946700.
KEGGiecj:Y75_p2170.
eco:b2209.
PATRICi32119777. VBIEscCol129921_2298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A38742.
RefSeqi NP_416713.1. NC_000913.3.
YP_490447.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AZZ X-ray 2.30 C/D 21-162 [» ]
1ECY X-ray 2.19 A 21-162 [» ]
1ECZ X-ray 2.68 A/B 21-162 [» ]
1EZS X-ray 2.30 A/B 21-162 [» ]
1EZU X-ray 2.40 A/B 21-162 [» ]
1FI8 X-ray 2.20 C/E 21-109 [» ]
D/F 105-162 [» ]
1ID5 X-ray 2.50 I 21-162 [» ]
1IFG X-ray 2.00 A 26-162 [» ]
1N8O X-ray 2.00 E 21-162 [» ]
1P0S X-ray 2.80 E 21-162 [» ]
1SLU X-ray 1.80 A 21-162 [» ]
1SLV X-ray 2.30 A 21-162 [» ]
1SLW X-ray 2.00 A 21-162 [» ]
1SLX X-ray 2.20 A 21-162 [» ]
1XX9 X-ray 2.20 C/D 21-162 [» ]
1XXD X-ray 2.91 C/D 21-162 [» ]
1XXF X-ray 2.60 C/D 21-162 [» ]
4IW4 X-ray 3.20 C/D 21-162 [» ]
4NIY X-ray 2.84 E/F/G/H 21-162 [» ]
ProteinModelPortali P23827.
SMRi P23827. Positions 21-162.
ModBasei Search...

Protein-protein interaction databases

IntActi P23827. 6 interactions.
MINTi MINT-276115.
STRINGi 511145.b2209.

Protein family/group databases

MEROPSi I11.001.

Proteomic databases

PaxDbi P23827.
PRIDEi P23827.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75269 ; AAC75269 ; b2209 .
BAA15992 ; BAA15992 ; BAA15992 .
GeneIDi 12933224.
946700.
KEGGi ecj:Y75_p2170.
eco:b2209.
PATRICi 32119777. VBIEscCol129921_2298.

Organism-specific databases

EchoBASEi EB0251.
EcoGenei EG10255. eco.

Phylogenomic databases

eggNOGi COG4574.
HOGENOMi HOG000263245.
KOi K08276.
OMAi RFRTWKV.
OrthoDBi EOG6P0711.
PhylomeDBi P23827.

Enzyme and pathway databases

BioCyci EcoCyc:EG10255-MONOMER.
ECOL316407:JW2197-MONOMER.

Miscellaneous databases

EvolutionaryTracei P23827.
PROi P23827.

Gene expression databases

Genevestigatori P23827.

Family and domain databases

Gene3Di 2.60.40.550. 1 hit.
4.10.1230.10. 1 hit.
HAMAPi MF_00706. Ecotin.
InterProi IPR027438. Ecotin_C.
IPR005658. Prot_inh_ecotin.
IPR023189. Prot_inh_ecotin_dom.
IPR023084. Prot_inh_ecotin_gammaproteobac.
[Graphical view ]
Pfami PF03974. Ecotin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006865. Prot_inh_ecotin. 1 hit.
SUPFAMi SSF49772. SSF49772. 1 hit.
ProtoNeti Search...

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 9, 2014
This is version 125 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

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