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Protein

Heat-labile enterotoxin IIB, A chain

Gene
N/A
Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 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 bindingi26 – 3914NADAdd
BLAST

GO - Molecular functioni

  1. catalytic activity Source: InterPro

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 IIB, A chain
Short name:
LT-IIB
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 263243Heat-labile enterotoxin IIB, A chainPRO_0000019354Add
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

DIPiDIP-6216N.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 298Combined sources
Helixi31 – 377Combined sources
Turni49 – 513Combined sources
Helixi59 – 646Combined sources
Beta strandi70 – 723Combined sources
Helixi84 – 9411Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi112 – 1143Combined sources
Helixi115 – 1195Combined sources
Helixi120 – 1223Combined sources
Helixi126 – 1283Combined sources
Beta strandi131 – 1344Combined sources
Helixi139 – 1413Combined sources
Beta strandi142 – 1498Combined sources
Helixi165 – 1684Combined sources
Helixi176 – 1805Combined sources
Helixi190 – 1934Combined sources
Helixi197 – 1993Combined sources
Helixi203 – 2053Combined sources
Helixi217 – 24832Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIIX-ray2.25A21-210[»]
C211-263[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43528.

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.

P43528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVISFFIS LFLISFPLYA NDYFRADSRT PDEVRRSGGL IPRGQDEAYE
60 70 80 90 100
RGTPININLY DHARGTATGN TRYNDGYVST TTTLRQAHFL GQNMLGGYNE
110 120 130 140 150
YYIYVVAAAP NLFDVNGVLG RYSPYPSENE YAALGGIPLS QIIGWYRVSF
160 170 180 190 200
GAIEGGMHRN RDYRRDLFRG LSAAPNEDGY RIAGFPDGFP AWEEVPWREF
210 220 230 240 250
APNSCLPNNK ASSDTTCASL TNKLSQHDLA DFKKYIKRKF TLMTLLSINN
260
DGFFSNNGGK DEL
Length:263
Mass (Da):29,519
Last modified:September 4, 2012 - v2
Checksum:i4F648DBDF99CA791
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ031712 Genomic DNA. Translation: AAA53285.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ031712 Genomic DNA. Translation: AAA53285.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIIX-ray2.25A21-210[»]
C211-263[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6216N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP43528.

Family and domain databases

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

Publicationsi

  1. "Cloning, nucleotide sequence, and hybridization studies of the type IIb heat-labile enterotoxin gene of Escherichia coli."
    Pickett C.L., Twiddy E.M., Coker C., Holmes R.K.
    J. Bacteriol. 171:4945-4952(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Isolate 41.
  2. Jobling M.G., Holmes R.K.
    Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 89.
  3. "Crystal structure of a new heat-labile enterotoxin, LT-IIb."
    van den Akker F., Sarfaty S., Twiddy E.M., Connell T.D., Holmes R.K., Hol W.G.J.
    Structure 4:665-678(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Entry informationi

Entry nameiE2BA_ECOLX
AccessioniPrimary (citable) accession number: P43528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: September 4, 2012
Last modified: November 25, 2014
This is version 64 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

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

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 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.