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P06717 (ELAP_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat-labile enterotoxin A chain
Alternative name(s):
LT-A, porcine
LTP-A
Gene names
Name:eltA
Synonyms:ltpA
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Heterohexamer of one A chain and of five B chains.

Sequence similarities

Belongs to the enterotoxin A family.

Ontologies

Keywords
   DomainSignal
   Molecular functionEnterotoxin
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncatalytic activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 258240Heat-labile enterotoxin A chain
PRO_0000019351

Regions

Nucleotide binding25 – 3915NAD

Sites

Active site1301

Amino acid modifications

Disulfide bond205 ↔ 217

Natural variations

Natural variant1301E → K in inactive mutant.

Experimental info

Mutagenesis251R → K: Abolishes toxicity. Ref.8
Mutagenesis711V → D or E: Abolishes toxicity. Ref.8
Mutagenesis721R → A or K: No effect. Ref.8
Mutagenesis771Y → M: No effect. Ref.8
Mutagenesis811S → K: Abolishes toxicity. Ref.8
Mutagenesis901A → E, H or R: No effect. Ref.8
Mutagenesis1151V → K: Abolishes toxicity. Ref.8
Mutagenesis1221Y → D or K: Abolishes toxicity. Ref.8
Mutagenesis1251H → E: Strongly reduces toxicity. Ref.8
Mutagenesis1281E → S: Abolishes toxicity. Ref.8
Mutagenesis1301E → S: Abolishes toxicity. Ref.8
Mutagenesis1321S → E or K: Abolishes toxicity. Ref.8
Mutagenesis2101R → N: No effect. Ref.8
Sequence conflict37 – 393SGG → FRS in CAA23532. Ref.3
Sequence conflict451Missing in CAA23532. Ref.3
Sequence conflict931S → Y in CAA23532. Ref.3
Sequence conflict100 – 11011TYYIYVIATAP → LTIYIVIA in CAA23532. Ref.3
Sequence conflict119 – 1202LG → IS in CAA23532. Ref.3
Sequence conflict1591R → G in AAB59161. Ref.4
Sequence conflict2071N → D in CAA23532. Ref.3

Secondary structure

.............................................. 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06717 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 2F0786442619F81F

FASTA25829,902
        10         20         30         40         50         60 
MKNITFIFFI LLASPLYANG DRLYRADSRP PDEIKRSGGL MPRGHNEYFD RGTQMNINLY 

        70         80         90        100        110        120 
DHARGTQTGF VRYDDGYVST SLSLRSAHLA GQSILSGYST YYIYVIATAP NMFNVNDVLG 

       130        140        150        160        170        180 
VYSPHPYEQE VSALGGIPYS QIYGWYRVNF GVIDERLHRN REYRDRYYRN LNIAPAEDGY 

       190        200        210        220        230        240 
RLAGFPPDHQ AWREEPWIHH APQGCGNSSR TITGDTCNEE TQNLSTIYLR EYQSKVKRQI 

       250 
FSDYQSEVDI YNRIRDEL 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRQLECA. I55231.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP06717.
SMRP06717. Positions 19-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06717. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001144. Enterotoxin_A.
[Graphical view]
PfamPF01375. Enterotoxin_a. 1 hit.
[Graphical view]
PRINTSPR00771. ENTEROTOXINA.
ProtoNetSearch...

Other

EvolutionaryTraceP06717.

Entry information

Entry nameELAP_ECOLX
AccessionPrimary (citable) accession number: P06717
Secondary accession number(s): P01554
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references