Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat-labile enterotoxin A chain

Gene

eltA

Organism
Escherichia coli
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1301

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi25 – 39NADAdd BLAST15

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25R → K: Abolishes toxicity. 1 Publication1
Mutagenesisi71V → D or E: Abolishes toxicity. 1 Publication1
Mutagenesisi72R → A or K: No effect. 1 Publication1
Mutagenesisi77Y → M: No effect. 1 Publication1
Mutagenesisi81S → K: Abolishes toxicity. 1 Publication1
Mutagenesisi90A → E, H or R: No effect. 1 Publication1
Mutagenesisi115V → K: Abolishes toxicity. 1 Publication1
Mutagenesisi122Y → D or K: Abolishes toxicity. 1 Publication1
Mutagenesisi125H → E: Strongly reduces toxicity. 1 Publication1
Mutagenesisi128E → S: Abolishes toxicity. 1 Publication1
Mutagenesisi130E → S: Abolishes toxicity. 1 Publication1
Mutagenesisi132S → E or K: Abolishes toxicity. 1 Publication1
Mutagenesisi210R → N: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000001935119 – 258Heat-labile enterotoxin A chainAdd BLAST240

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactor.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 29Combined sources7
Helixi31 – 37Combined sources7
Beta strandi47 – 49Combined sources3
Beta strandi51 – 53Combined sources3
Helixi59 – 64Combined sources6
Beta strandi70 – 72Combined sources3
Beta strandi77 – 83Combined sources7
Helixi84 – 94Combined sources11
Helixi95 – 97Combined sources3
Beta strandi99 – 106Combined sources8
Beta strandi112 – 114Combined sources3
Helixi115 – 119Combined sources5
Helixi120 – 122Combined sources3
Helixi126 – 128Combined sources3
Beta strandi130 – 134Combined sources5
Helixi139 – 141Combined sources3
Beta strandi142 – 149Combined sources8
Beta strandi152 – 159Combined sources8
Helixi165 – 170Combined sources6
Helixi176 – 179Combined sources4
Helixi180 – 182Combined sources3
Helixi190 – 193Combined sources4
Helixi197 – 200Combined sources4
Helixi215 – 240Combined sources26
Helixi241 – 244Combined sources4
Helixi250 – 253Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

        10         20         30         40         50
MKNITFIFFI LLASPLYANG DRLYRADSRP PDEIKRSGGL MPRGHNEYFD
60 70 80 90 100
RGTQMNINLY DHARGTQTGF VRYDDGYVST SLSLRSAHLA GQSILSGYST
110 120 130 140 150
YYIYVIATAP NMFNVNDVLG VYSPHPYEQE VSALGGIPYS QIYGWYRVNF
160 170 180 190 200
GVIDERLHRN REYRDRYYRN LNIAPAEDGY RLAGFPPDHQ AWREEPWIHH
210 220 230 240 250
APQGCGNSSR TITGDTCNEE TQNLSTIYLR EYQSKVKRQI FSDYQSEVDI

YNRIRDEL
Length:258
Mass (Da):29,902
Last modified:January 1, 1988 - v1
Checksum:i2F0786442619F81F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37 – 39SGG → FRS in CAA23532 (PubMed:6279611).Curated3
Sequence conflicti45Missing in CAA23532 (PubMed:6279611).Curated1
Sequence conflicti93S → Y in CAA23532 (PubMed:6279611).Curated1
Sequence conflicti100 – 110TYYIYVIATAP → LTIYIVIA in CAA23532 (PubMed:6279611).CuratedAdd BLAST11
Sequence conflicti119 – 120LG → IS in CAA23532 (PubMed:6279611).Curated2
Sequence conflicti159R → G in AAB59161 (PubMed:2266142).Curated1
Sequence conflicti207N → D in CAA23532 (PubMed:6279611).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti130E → K in inactive mutant. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
RefSeqiWP_042634421.1. NZ_LVNP01000056.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
RefSeqiWP_042634421.1. NZ_LVNP01000056.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06717. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06717.

Family and domain databases

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

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: November 2, 2016
This is version 90 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

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.