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P06717

- ELAP_ECOLX

UniProt

P06717 - ELAP_ECOLX

Protein

Heat-labile enterotoxin A chain

Gene

eltA

Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei130 – 1301

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi25 – 3915NADAdd
    BLAST

    GO - Molecular functioni

    1. catalytic activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Enterotoxin, Toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat-labile enterotoxin A chain
    Alternative name(s):
    LT-A, porcine
    LTP-A
    Gene namesi
    Name:eltA
    Synonyms:ltpA
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251R → K: Abolishes toxicity. 1 Publication
    Mutagenesisi71 – 711V → D or E: Abolishes toxicity. 1 Publication
    Mutagenesisi72 – 721R → A or K: No effect. 1 Publication
    Mutagenesisi77 – 771Y → M: No effect. 1 Publication
    Mutagenesisi81 – 811S → K: Abolishes toxicity. 1 Publication
    Mutagenesisi90 – 901A → E, H or R: No effect. 1 Publication
    Mutagenesisi115 – 1151V → K: Abolishes toxicity. 1 Publication
    Mutagenesisi122 – 1221Y → D or K: Abolishes toxicity. 1 Publication
    Mutagenesisi125 – 1251H → E: Strongly reduces toxicity. 1 Publication
    Mutagenesisi128 – 1281E → S: Abolishes toxicity. 1 Publication
    Mutagenesisi130 – 1301E → S: Abolishes toxicity. 1 Publication
    Mutagenesisi132 – 1321S → E or K: Abolishes toxicity. 1 Publication
    Mutagenesisi210 – 2101R → N: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 258240Heat-labile enterotoxin A chainPRO_0000019351Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi205 ↔ 217

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterohexamer of one A chain and of five B chains.

    Protein-protein interaction databases

    IntActiP06717. 1 interaction.

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 297
    Helixi31 – 377
    Beta strandi47 – 493
    Beta strandi51 – 533
    Helixi59 – 646
    Beta strandi70 – 723
    Beta strandi77 – 837
    Helixi84 – 9411
    Helixi95 – 973
    Beta strandi99 – 1068
    Beta strandi112 – 1143
    Helixi115 – 1195
    Helixi120 – 1223
    Helixi126 – 1283
    Beta strandi130 – 1345
    Helixi139 – 1413
    Beta strandi142 – 1498
    Beta strandi152 – 1598
    Helixi165 – 1706
    Helixi176 – 1794
    Helixi180 – 1823
    Helixi190 – 1934
    Helixi197 – 2004
    Helixi215 – 24026
    Helixi241 – 2444
    Helixi250 – 2534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HTLX-ray2.50A19-209[»]
    C210-258[»]
    1LT3X-ray2.00A19-258[»]
    1LT4X-ray2.00A19-251[»]
    1LTAX-ray2.20A19-206[»]
    C210-258[»]
    1LTBX-ray2.60A22-206[»]
    C210-254[»]
    1LTGX-ray2.40A19-209[»]
    C210-258[»]
    1LTIX-ray2.13A19-210[»]
    C211-258[»]
    1LTSX-ray1.95A22-206[»]
    C214-254[»]
    1LTTX-ray2.30A22-206[»]
    C214-254[»]
    ProteinModelPortaliP06717.
    SMRiP06717. Positions 19-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06717.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the enterotoxin A family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR001144. Enterotoxin_A.
    [Graphical view]
    PfamiPF01375. Enterotoxin_a. 1 hit.
    [Graphical view]
    PRINTSiPR00771. ENTEROTOXINA.

    Sequencei

    Sequence statusi: Complete.

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

    P06717-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNITFIFFI LLASPLYANG DRLYRADSRP PDEIKRSGGL MPRGHNEYFD    50
    RGTQMNINLY DHARGTQTGF VRYDDGYVST SLSLRSAHLA GQSILSGYST 100
    YYIYVIATAP NMFNVNDVLG VYSPHPYEQE VSALGGIPYS QIYGWYRVNF 150
    GVIDERLHRN REYRDRYYRN LNIAPAEDGY RLAGFPPDHQ AWREEPWIHH 200
    APQGCGNSSR TITGDTCNEE TQNLSTIYLR EYQSKVKRQI FSDYQSEVDI 250
    YNRIRDEL 258
    Length:258
    Mass (Da):29,902
    Last modified:January 1, 1988 - v1
    Checksum:i2F0786442619F81F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 393SGG → FRS in CAA23532. (PubMed:6279611)Curated
    Sequence conflicti45 – 451Missing in CAA23532. (PubMed:6279611)Curated
    Sequence conflicti93 – 931S → Y in CAA23532. (PubMed:6279611)Curated
    Sequence conflicti100 – 11011TYYIYVIATAP → LTIYIVIA in CAA23532. (PubMed:6279611)CuratedAdd
    BLAST
    Sequence conflicti119 – 1202LG → IS in CAA23532. (PubMed:6279611)Curated
    Sequence conflicti159 – 1591R → G in AAB59161. (PubMed:2266142)Curated
    Sequence conflicti207 – 2071N → D in CAA23532. (PubMed:6279611)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti130 – 1301E → K in inactive mutant.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15361 Genomic DNA. Translation: AAA24791.1.
    M15362 Genomic DNA. Translation: AAA24793.1.
    M35581 Genomic DNA. Translation: AAA98202.1.
    V00275 Genomic DNA. Translation: CAA23532.1.
    M57244 Genomic DNA. Translation: AAB59161.1.
    M61015 Genomic DNA. Translation: AAA24335.1.
    PIRiI55231. QLECA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15361 Genomic DNA. Translation: AAA24791.1 .
    M15362 Genomic DNA. Translation: AAA24793.1 .
    M35581 Genomic DNA. Translation: AAA98202.1 .
    V00275 Genomic DNA. Translation: CAA23532.1 .
    M57244 Genomic DNA. Translation: AAB59161.1 .
    M61015 Genomic DNA. Translation: AAA24335.1 .
    PIRi I55231. QLECA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HTL X-ray 2.50 A 19-209 [» ]
    C 210-258 [» ]
    1LT3 X-ray 2.00 A 19-258 [» ]
    1LT4 X-ray 2.00 A 19-251 [» ]
    1LTA X-ray 2.20 A 19-206 [» ]
    C 210-258 [» ]
    1LTB X-ray 2.60 A 22-206 [» ]
    C 210-254 [» ]
    1LTG X-ray 2.40 A 19-209 [» ]
    C 210-258 [» ]
    1LTI X-ray 2.13 A 19-210 [» ]
    C 211-258 [» ]
    1LTS X-ray 1.95 A 22-206 [» ]
    C 214-254 [» ]
    1LTT X-ray 2.30 A 22-206 [» ]
    C 214-254 [» ]
    ProteinModelPortali P06717.
    SMRi P06717. Positions 19-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P06717. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P06717.

    Family and domain databases

    InterProi IPR001144. Enterotoxin_A.
    [Graphical view ]
    Pfami PF01375. Enterotoxin_a. 1 hit.
    [Graphical view ]
    PRINTSi PR00771. ENTEROTOXINA.
    ProtoNeti Search...

    Publicationsi

    1. "Evolutionary origin of pathogenic determinants in enterotoxigenic Escherichia coli and Vibrio cholerae O1."
      Yamamoto T., Gojobori T., Yokota T.
      J. Bacteriol. 169:1352-1357(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Isolate P307 / ETEC and Isolate PCG86 / ETEC.
    2. "A comparison of the nucleotide sequence of the A subunit of heat-labile enterotoxin and cholera toxin."
      Dykes C.W., Halliday I.J., Hobden A.N., Read M.J., Harford S.
      FEMS Microbiol. Lett. 26:171-174(1985)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Isolate P307 / ETEC.
    3. "Escherichia coli heat-labile enterotoxin. Nucleotide sequence of the A subunit gene."
      Spicer E.K., Noble J.A.
      J. Biol. Chem. 257:5716-5721(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Isolate P307 / ETEC.
    4. "A single amino acid substitution in the A subunit of Escherichia coli enterotoxin results in a loss of its toxic activity."
      Tsuji T., Inoue T., Miyama A., Okamoto K., Honda T., Miwatani T.
      J. Biol. Chem. 265:22520-22525(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-258.
      Strain: Isolate P307 / ETEC.
    5. Trachman J.D., Maas W.K.
      Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    6. "Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli."
      Sixma T.K., Pronk S.E., Kalk K.H., Wartna E.S., van Zanten B.A.M., Witholt B., Hol W.G.J.
      Nature 351:371-377(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    7. "Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin."
      Sixma T.K., van Zanten B.A.M., Dauter Z., Hol W.G.J.
      J. Mol. Biol. 230:890-918(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    8. "Probing the structure-activity relationship of Escherichia coli LT-A by site-directed mutagenesis."
      Pizza M., Domenighini M., Hol W.G.J., Giannelli V., Fontana M.R., Giuliani M.M., Magagnoli C., Peppoloni S., Manetti R., Rappuoli R.
      Mol. Microbiol. 14:51-60(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 19-258, MUTAGENESIS OF ARG-25; VAL-71; ARG-72; TYR-77; SER-81; ALA-90; VAL-115; TYR-122; HIS-125; GLU-128; GLU-130; SER-132 AND ARG-210.
    9. "Identification of errors among database sequence entries and comparison of correct amino acid sequences for the heat-labile enterotoxins of Escherichia coli and Vibrio cholerae."
      Domenighini M., Pizza M., Jobling M.G., Holmes R.K., Rappuoli R.
      Mol. Microbiol. 15:1165-1167(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISCUSSION OF SEQUENCE.

    Entry informationi

    Entry nameiELAP_ECOLX
    AccessioniPrimary (citable) accession number: P06717
    Secondary accession number(s): P01554
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 83 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3