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Protein

Heat-labile enterotoxin B chain

Gene

eltB

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 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.

GO - Biological processi

  • killing of cells of other organism Source: CACAO
  • pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Enterotoxin, Toxin

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 124103Heat-labile enterotoxin B chainPRO_0000019355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 107

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterohexamer of one A chain and of five B chains.

Protein-protein interaction databases

DIPiDIP-36815N.
IntActiP32890. 1 interaction.

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 305Combined sources
Beta strandi36 – 438Combined sources
Beta strandi46 – 516Combined sources
Beta strandi58 – 625Combined sources
Beta strandi68 – 714Combined sources
Beta strandi76 – 783Combined sources
Helixi82 – 9817Combined sources
Beta strandi103 – 12321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJRX-ray1.30D/E/F/G/H22-124[»]
1EEFX-ray1.80D/E/F/G/H/L/M/N/O/P22-124[»]
1EFIX-ray1.60D/E/F/G/H22-124[»]
1FD7X-ray1.80D/E/F/G/H/L/M/N/O/P22-124[»]
1HTLX-ray2.50D/E/F/G/H22-124[»]
1JQYX-ray2.14D/E/F/G/H/L/M/N/O/P/V/W/X/Y/Z22-124[»]
1LT3X-ray2.00D/E/F/G/H22-124[»]
1LT4X-ray2.00D/E/F/G/H22-124[»]
1LT5X-ray1.70D/E/F/G/H22-124[»]
1LT6X-ray2.20D/E/F/G/H/L/M/N/O/P22-124[»]
1LTAX-ray2.20D/E/F/G/H22-124[»]
1LTBX-ray2.60D/E/F/G/H22-124[»]
1LTGX-ray2.40D/E/F/G/H22-124[»]
1LTIX-ray2.13D/E/F/G/H22-124[»]
1LTSX-ray1.95D/E/F/G/H22-124[»]
1LTTX-ray2.30D/E/F/G/H22-124[»]
1PZIX-ray1.99D/E/F/G/H22-124[»]
1TETX-ray2.30P71-85[»]
2XRQX-ray2.40D/E/F/G/H22-124[»]
2XRSX-ray1.81D/E/F/G/H/L/M/N/O/P22-124[»]
ProteinModelPortaliP32890.
SMRiP32890. Positions 22-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32890.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR008992. Enterotoxin.
IPR001835. Enterotoxin_B.
[Graphical view]
PfamiPF01376. Enterotoxin_b. 1 hit.
[Graphical view]
PRINTSiPR00772. ENTEROTOXINB.
ProDomiPD012805. Enterotoxin_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50203. SSF50203. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P32890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKVKCYVLF TALLSSLYAH GAPQTITELC SEYRNTQIYT INDKILSYTE
60 70 80 90 100
SMAGKREMVI ITFKSGETFQ VEVPGSQHID SQKKAIERMK DTLRITYLTE
110 120
TKIDKLCVWN NKTPNSIAAI SMKN
Length:124
Mass (Da):14,133
Last modified:November 1, 1995 - v2
Checksum:i6DB7DE58395EA70D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961T → A in strain: 240-3 / ETEC.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17873 Genomic DNA. Translation: AAA98065.1.
M15363 Genomic DNA. Translation: AAA24792.1.
M17101 Genomic DNA. Translation: AAA23973.1.
PIRiA01820. QLECB.
RefSeqiWP_015675362.1. NZ_LBBN01000054.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17873 Genomic DNA. Translation: AAA98065.1.
M15363 Genomic DNA. Translation: AAA24792.1.
M17101 Genomic DNA. Translation: AAA23973.1.
PIRiA01820. QLECB.
RefSeqiWP_015675362.1. NZ_LBBN01000054.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJRX-ray1.30D/E/F/G/H22-124[»]
1EEFX-ray1.80D/E/F/G/H/L/M/N/O/P22-124[»]
1EFIX-ray1.60D/E/F/G/H22-124[»]
1FD7X-ray1.80D/E/F/G/H/L/M/N/O/P22-124[»]
1HTLX-ray2.50D/E/F/G/H22-124[»]
1JQYX-ray2.14D/E/F/G/H/L/M/N/O/P/V/W/X/Y/Z22-124[»]
1LT3X-ray2.00D/E/F/G/H22-124[»]
1LT4X-ray2.00D/E/F/G/H22-124[»]
1LT5X-ray1.70D/E/F/G/H22-124[»]
1LT6X-ray2.20D/E/F/G/H/L/M/N/O/P22-124[»]
1LTAX-ray2.20D/E/F/G/H22-124[»]
1LTBX-ray2.60D/E/F/G/H22-124[»]
1LTGX-ray2.40D/E/F/G/H22-124[»]
1LTIX-ray2.13D/E/F/G/H22-124[»]
1LTSX-ray1.95D/E/F/G/H22-124[»]
1LTTX-ray2.30D/E/F/G/H22-124[»]
1PZIX-ray1.99D/E/F/G/H22-124[»]
1TETX-ray2.30P71-85[»]
2XRQX-ray2.40D/E/F/G/H22-124[»]
2XRSX-ray1.81D/E/F/G/H/L/M/N/O/P22-124[»]
ProteinModelPortaliP32890.
SMRiP32890. Positions 22-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36815N.
IntActiP32890. 1 interaction.

Chemistry

DrugBankiDB03793. Benzoic Acid.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP32890.

Family and domain databases

InterProiIPR008992. Enterotoxin.
IPR001835. Enterotoxin_B.
[Graphical view]
PfamiPF01376. Enterotoxin_b. 1 hit.
[Graphical view]
PRINTSiPR00772. ENTEROTOXINB.
ProDomiPD012805. Enterotoxin_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50203. SSF50203. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence homology between cholera toxin and Escherichia coli heat-labile toxin."
    Dallas W.S., Falkow S.
    Nature 288:499-501(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Isolate P307 / ETEC.
  2. "Nucleotide sequence comparison between heat-labile toxin B-subunit cistrons from Escherichia coli of human and porcine origin."
    Leong J., Vinal A.C., Dallas W.S.
    Infect. Immun. 48:73-77(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 28 AND 64.
    Strain: Isolate P307 / ETEC.
  3. "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 PCG86 / ETEC.
  4. "A functional interaction between the signal peptide and the translation apparatus is detected by the use of a single point mutation which blocks translocation across mammalian endoplasmic reticulum."
    Ibrahimi I., Gentz R.
    J. Biol. Chem. 262:10189-10194(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  5. "A unique amino acid sequence of the B subunit of a heat-labile enterotoxin isolated from a human enterotoxigenic Escherichia coli."
    Tsuji T., Iida T., Honda T., Miwatani T., Nagahama M., Sakurai J., Wada K., Matsubara H.
    Microb. Pathog. 2:381-390(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-124.
    Strain: 240-3 / ETEC.
  6. "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).
  7. "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).
  8. "Anchor-based design of improved cholera toxin and E. coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes."
    Pickens J.C., Merritt E.A., Ahn M., Verlinde C.L.M.J., Hol W.G.J., Fan E.
    Chem. Biol. 9:215-224(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS).
  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 nameiELBP_ECOLX
AccessioniPrimary (citable) accession number: P32890
Secondary accession number(s): P01557, P13768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: January 20, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.