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Protein

Pertussis toxin subunit 1

Gene

ptxA

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD+ into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors.

Miscellaneous

Thiol:disulfide oxidoreductases DsbA and DsbB are required for periplasmic toxin assembly, whereas DbsC is important for extracellular toxin secretion.
Experiments with temporal expression of PTX indicate that holotoxin secretion is at a rate of 3 molecules/min/cell. Also, more of toxin chains S1, S2 and S3 are produced than secreted; one half of each chain is incorporated into holotoxin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei60NAD1
Active sitei691
Active sitei1631

GO - Molecular functioni

Keywordsi

Molecular functionGlycosyltransferase, Toxin, Transferase
Biological processVirulence
LigandNAD

Enzyme and pathway databases

BioCyciBPER257313:BP3783-MONOMER

Protein family/group databases

TCDBi1.C.72.1.1 the pertussis toxin (ptx) family

Names & Taxonomyi

Protein namesi
Recommended name:
Pertussis toxin subunit 1
Short name:
PTX S1
Alternative name(s):
Islet-activating protein S1
Short name:
IAP S1
NAD-dependent ADP-ribosyltransferase (EC:2.4.2.-)
Gene namesi
Name:ptxA
Ordered Locus Names:BP3783
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000002676 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication
  • Note: The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secretion of assembled toxin through the outer membrane.

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Currently used in vaccines available under the names Daptacel (Sanofi Pasteur), Infanrix (GlaxoSmithKline), Pediarix (GlaxoSmithKline), TriHIBit (Sanofi Pasteur) and Tripedia (Sanofi Pasteur).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi75C → G: 38% of wild-type NAD-glycohydrolase activity. 1 Publication1
Mutagenesisi75C → S: 33% of wild-type NAD-glycohydrolase activity. 1 Publication1
Mutagenesisi75Missing : More than 100-fold reduction of NAD-glycohydrolase activity. 1 Publication1
Mutagenesisi88S → G: No functional toxin produced although some mature size S1 protein accumulates in the periplasm. 1 Publication1
Mutagenesisi89S → G: Very low amount of final toxin secreted; approximately 50% of wild-type toxin level accumulate in the periplasm despite near wild-type levels of mature size S1 in the periplasm. 1 Publication1
Mutagenesisi90S → G: Very low amount of final toxin secreted; approximately 50% of wild-type toxin level accumulate in the periplasm despite near wild-type levels of mature size S1 in the periplasm. 1 Publication1
Mutagenesisi91R → K: Very low amounts of final toxin secreted; about 60% of wild-type toxin levels accumulate in the periplasm. Near wild-type levels of mature size S1 in the periplasm. 1 Publication1
Mutagenesisi163E → D: Reduction of several orders of magnitude of enzymatic activity. 1 Publication1
Mutagenesisi163Missing : Dramatic decrease in enzymatic activity. 1 Publication1
Mutagenesisi269Missing : Affects both protein stability and outer membrane targeting. 1 Publication1

Keywords - Diseasei

Whooping cough

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Add BLAST34
ChainiPRO_000001935935 – 269Pertussis toxin subunit 1Add BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi75 ↔ 235

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP04977

Expressioni

Inductioni

Activated by the two-component regulatory system BvgS/BvgA.

Interactioni

Subunit structurei

Pertussis toxin contains five different chains, S1-S5. They are organized into 2 functional subunits: A, composed of S1 (which is toxic) and B, containing S2, S3, S5, and two copies of S4 (B binds to the membrane receptors). Dimers of S2-S4 and S3-S4 are held together by S5.1 Publication

Protein-protein interaction databases

STRINGi257313.BP3783

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP04977
SMRiP04977
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04977

Family & Domainsi

Domaini

The region which spans amino acids 42-49 is required for enzymatic activity and contributes to the formation of a potentially important antigenic determinant.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106DF6 Bacteria
ENOG410XY7Z LUCA
HOGENOMiHOG000154667
KOiK11023
OMAiYIYQIRA

Family and domain databases

InterProiView protein in InterPro
IPR003898 Borpert_toxA
PfamiView protein in Pfam
PF02917 Pertussis_S1, 1 hit
PRINTSiPR01395 BORPETOXINA

Sequencei

Sequence statusi: Complete.

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

P04977-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRCTRAIRQT ARTGWLTWLA ILAVTAPVTS PAWADDPPAT VYRYDSRPPE
60 70 80 90 100
DVFQNGFTAW GNNDNVLDHL TGRSCQVGSS NSAFVSTSSS RRYTEVYLEH
110 120 130 140 150
RMQEAVEAER AGRGTGHFIG YIYEVRADNN FYGAASSYFE YVDTYGDNAG
160 170 180 190 200
RILAGALATY QSEYLAHRRI PPENIRRVTR VYHNGITGET TTTEYSNARY
210 220 230 240 250
VSQQTRANPN PYTSRRSVAS IVGTLVRMAP VIGACMARQA ESSEAMAAWS
260
ERAGEAMVLV YYESIAYSF
Length:269
Mass (Da):29,974
Last modified:August 13, 1987 - v1
Checksum:iF6C88C16DA6B08AB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti68D → E in strain: 10536, CZ, 18323 and B6. 1
Natural varianti129N → S in strain: CS. 1
Natural varianti196S → P in strain: CZ and 18323. 1
Natural varianti228M → I in strain: 287, Al1561, B572, CHANG and HAV. 1
Natural varianti232I → M in strain: CZ and 18323. 1
Natural varianti232I → V in strain: 10536 and B6. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14378 Genomic DNA Translation: AAA83980.1
M13223 Genomic DNA Translation: AAA22981.1
X16347 Genomic DNA Translation: CAA34397.1
AJ245366 Genomic DNA Translation: CAB51472.1
AJ245367 Genomic DNA Translation: CAB51542.1
AJ245368 Genomic DNA Translation: CAB51543.1
AJ506996 Genomic DNA Translation: CAD44970.1
AJ006151 Genomic DNA Translation: CAA06893.1
AJ006153 Genomic DNA Translation: CAA06895.1
AJ006155 Genomic DNA Translation: CAA06897.1
AJ006157 Genomic DNA Translation: CAA06899.1
AJ006159 Genomic DNA Translation: CAA06901.1
AJ007363 Genomic DNA Translation: CAA07478.1
AJ007364 Genomic DNA Translation: CAA07479.1
AJ506994 Genomic DNA Translation: CAD44968.1
AJ506995 Genomic DNA Translation: CAD44969.1
AY879289 Genomic DNA Translation: AAW72734.1
AJ920066 Genomic DNA Translation: CAI72620.1
BX640422 Genomic DNA Translation: CAE44038.1
PIRiA24144 WEBR1P
A24394 WEBR11
RefSeqiNP_882282.1, NC_002929.2
WP_010931648.1, NC_002929.2

Genome annotation databases

EnsemblBacteriaiCAE44038; CAE44038; BP3783
GeneIDi2665068
KEGGibpe:BP3783
PATRICifig|257313.5.peg.4087

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14378 Genomic DNA Translation: AAA83980.1
M13223 Genomic DNA Translation: AAA22981.1
X16347 Genomic DNA Translation: CAA34397.1
AJ245366 Genomic DNA Translation: CAB51472.1
AJ245367 Genomic DNA Translation: CAB51542.1
AJ245368 Genomic DNA Translation: CAB51543.1
AJ506996 Genomic DNA Translation: CAD44970.1
AJ006151 Genomic DNA Translation: CAA06893.1
AJ006153 Genomic DNA Translation: CAA06895.1
AJ006155 Genomic DNA Translation: CAA06897.1
AJ006157 Genomic DNA Translation: CAA06899.1
AJ006159 Genomic DNA Translation: CAA06901.1
AJ007363 Genomic DNA Translation: CAA07478.1
AJ007364 Genomic DNA Translation: CAA07479.1
AJ506994 Genomic DNA Translation: CAD44968.1
AJ506995 Genomic DNA Translation: CAD44969.1
AY879289 Genomic DNA Translation: AAW72734.1
AJ920066 Genomic DNA Translation: CAI72620.1
BX640422 Genomic DNA Translation: CAE44038.1
PIRiA24144 WEBR1P
A24394 WEBR11
RefSeqiNP_882282.1, NC_002929.2
WP_010931648.1, NC_002929.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCPX-ray2.70A/G35-269[»]
1PRTX-ray2.90A/G36-269[»]
1PTOX-ray3.50A/G26-269[»]
ProteinModelPortaliP04977
SMRiP04977
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP3783

Protein family/group databases

TCDBi1.C.72.1.1 the pertussis toxin (ptx) family

Proteomic databases

PRIDEiP04977

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE44038; CAE44038; BP3783
GeneIDi2665068
KEGGibpe:BP3783
PATRICifig|257313.5.peg.4087

Phylogenomic databases

eggNOGiENOG4106DF6 Bacteria
ENOG410XY7Z LUCA
HOGENOMiHOG000154667
KOiK11023
OMAiYIYQIRA

Enzyme and pathway databases

BioCyciBPER257313:BP3783-MONOMER

Miscellaneous databases

EvolutionaryTraceiP04977

Family and domain databases

InterProiView protein in InterPro
IPR003898 Borpert_toxA
PfamiView protein in Pfam
PF02917 Pertussis_S1, 1 hit
PRINTSiPR01395 BORPETOXINA
ProtoNetiSearch...

Entry informationi

Entry nameiTOX1_BORPE
AccessioniPrimary (citable) accession number: P04977
Secondary accession number(s): O69258
, O70057, Q599G4, Q5EIB9, Q93V22
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 7, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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