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P23827

- ECOT_ECOLI

UniProt

P23827 - ECOT_ECOLI

Protein

Ecotin

Gene

eco

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

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

    GO - Biological processi

    1. negative regulation of endopeptidase activity Source: GOC

    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

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: EcoCyc

    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.

    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

    1
    162
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 126 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