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P06717

- ELAP_ECOLX

UniProt

P06717 - ELAP_ECOLX

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Protein
Heat-labile enterotoxin A chain
Gene
eltA, ltpA
Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 3915NAD
Add
BLAST

GO - Molecular functioni

  1. catalytic activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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 – 1818
Add
BLAST
Chaini19 – 258240Heat-labile enterotoxin A chain
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP06717.

Family & Domainsi

Sequence similaritiesi

Belongs to the enterotoxin A family.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 393SGG → FRS in CAA23532. 1 Publication
Sequence conflicti45 – 451Missing in CAA23532. 1 Publication
Sequence conflicti93 – 931S → Y in CAA23532. 1 Publication
Sequence conflicti100 – 11011TYYIYVIATAP → LTIYIVIA in CAA23532. 1 Publication
Add
BLAST
Sequence conflicti119 – 1202LG → IS in CAA23532. 1 Publication
Sequence conflicti159 – 1591R → G in AAB59161. 1 Publication
Sequence conflicti207 – 2071N → D in CAA23532. 1 Publication

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...

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: April 16, 2014
This is version 82 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

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