TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


1.C.72.1.1
Pertussis toxin

Accession Number:P04977
Protein Name:PTX S1
Length:269
Molecular Weight:29974.00
Species:Bordetella pertussis [520]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Secreted1
Substrate toxin

Cross database links:

RefSeq: NP_882282.1   
Entrez Gene ID: 2665068   
Pfam: PF02917   
BioCyc: BPER257313:BP3783-MONOMER   
KEGG: bpe:BP3783   

Gene Ontology

GO:0005576 C:extracellular region
GO:0003950 F:NAD+ ADP-ribosyltransferase activity
GO:0009405 P:pathogenesis

References (19)

[1] “Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication.”  Nicosia A.et.al.   2873570
[2] “Pertussis toxin gene: nucleotide sequence and genetic organization.”  Locht C.et.al.   3704651
[3] “A unique sequence of the Bordetella pertussis toxin operon.”  Loosmore S.M.et.al.   2554254
[4] “Polymorphism in the Bordetella pertussis virulence factors P.69/pertactin and pertussis toxin in The Netherlands: temporal trends and evidence for vaccine-driven evolution.”  Mooi F.R.et.al.   9453625
[5] “Intranasal murine model of Bordetella pertussis infection: II. Sequence variation and protection induced by a tricomponent acellular vaccine.”  Boursaux-Eude C.et.al.   10418915
[6] “Temporal trends in circulating Bordetella pertussis strains in Australia.”  Poynten M.et.al.   15061492
[7] “Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.”  Parkhill J.et.al.   12910271
[8] “Identification of a region in the S1 subunit of pertussis toxin that is required for enzymatic activity and that contributes to the formation of a neutralizing antigenic determinant.”  Cieplak W.et.al.   2455296
[9] “Identification of an active-site residue in subunit S1 of pertussis toxin by photocrosslinking to NAD.”  Cockle S.A.et.al.   2737291
[10] “Role of tryptophan 26 in the NAD glycohydrolase reaction of the S-1 subunit of pertussis toxin.”  Cortina G.et.al.   2551899
[11] “Further analysis of the sequence of the S1 subunit of pertussis toxin.”  Pizza M.et.al.   1997420
[12] “A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit.”  Locht C.et.al.   8527486
[13] “Synergistic binding of RNA polymerase and BvgA phosphate to the pertussis toxin promoter of Bordetella pertussis.”  Boucher P.E.et.al.   7592424
[14] “Mutations in the S1 subunit of pertussis toxin that affect secretion.”  Craig-Mylius K.A.et.al.   10678938
[15] “Membrane localization of the S1 subunit of pertussis toxin in Bordetella pertussis and implications for pertussis toxin secretion.”  Farizo K.M.et.al.   11854200
[16] “DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis.”  Stenson T.H.et.al.   11953363
[17] “Temporal expression of pertussis toxin and Ptl secretion proteins by Bordetella pertussis.”  Rambow-Larsen A.A.et.al.   14679223
[18] “The crystal structure of pertussis toxin.”  Stein P.E.et.al.   8075982
[19] “Crystal structure of the pertussis toxin-ATP complex: a molecular sensor.”  Hazes B.et.al.   8637000
Structure:
1BCP   1PRT   1PTO   6RO0     

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MRCTRAIRQT ARTGWLTWLA ILAVTAPVTS PAWADDPPAT VYRYDSRPPE DVFQNGFTAW 
61:	GNNDNVLDHL TGRSCQVGSS NSAFVSTSSS RRYTEVYLEH RMQEAVEAER AGRGTGHFIG 
121:	YIYEVRADNN FYGAASSYFE YVDTYGDNAG RILAGALATY QSEYLAHRRI PPENIRRVTR 
181:	VYHNGITGET TTTEYSNARY VSQQTRANPN PYTSRRSVAS IVGTLVRMAP VIGACMARQA 
241:	ESSEAMAAWS ERAGEAMVLV YYESIAYSF