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O06522 (CDTA_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytolethal distending toxin subunit A
Short name=CDT A
Gene names
Name:cdtA
Ordered Locus Names:HD_0902
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

CDTs are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of CdtB. Ref.3

Subunit structure

Heterotrimer of 3 subunits, CdtA, CdtB and CdtC. Ref.3

Subcellular location

Cell outer membrane; Lipid-anchor Probable.

Sequence similarities

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell outer membrane
Membrane
   DomainSignal
   LigandLectin
   Molecular functionToxin
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionsugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 223208Cytolethal distending toxin subunit A
PRO_0000013371

Regions

Domain123 – 21290Ricin B-type lectin
Region91 – 10212Mediates binding to target cells Probable

Amino acid modifications

Lipidation161N-palmitoyl cysteine Potential
Lipidation161S-diacylglycerol cysteine Potential

Experimental info

Mutagenesis911W → G: Abolishes toxicity towards intact cells; when associated with G-98; G-100 and G-102. Ref.3
Mutagenesis981W → G: Abolishes toxicity towards intact cells; when associated with G-91; G-100 and G-102. Ref.3
Mutagenesis1001W → G: Abolishes toxicity towards intact cells; when associated with G-91; G-98 and G-102. Ref.3
Mutagenesis1021Y → G: Abolishes toxicity towards intact cells; when associated with G-91; G-98 and G-100. Ref.3

Secondary structure

1 ........................................ 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O06522 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 5CA68F05958CD56D

FASTA22324,664
        10         20         30         40         50         60 
MKKFLPSLLL MGSVACSSNQ RMNDYSQPES QSDLAPKSST IQPQPQPLLS KTPSMSLNLL 

        70         80         90        100        110        120 
SSSGPNRQVL PSEPSNFMTL MGQNGALLTV WALAKRNWLW AYPNIYSQDF GNIRNWKMEP 

       130        140        150        160        170        180 
GKHREYFRFV NQSLGTCVEA YGNGLIHDIC SLDKLAQEFE LLPTDSGAVV IKSVSQGRCV 

       190        200        210        220 
TYNPVSTTFY STVTLSVCDG ATEPSRDQTW YLAPPVLEAT AVN

« Hide

References

« Hide 'large scale' references
[1]"A diffusible cytotoxin of Haemophilus ducreyi."
Cope L.D., Lumbley S., Latimer J.L., Klesney-Tait J., Stevens M.K., Johnson L.S., Purven M., Munson R.S. Jr., Lagergard T., Radolf J.D., Hansen E.J.
Proc. Natl. Acad. Sci. U.S.A. 94:4056-4061(1997) [PubMed: 9108104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 35000HP / ATCC 700724.
[2]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.
[3]"Assembly and function of a bacterial genotoxin."
Nesic D., Hsu Y., Stebbins C.E.
Nature 429:429-433(2004) [PubMed: 15164065] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-223, FUNCTION, MUTAGENESIS OF TRP-91; TRP-98; TRP-100 AND TYR-102, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U53215 Genomic DNA. Translation: AAB57725.1.
AE017143 Genomic DNA. Translation: AAP95786.1.
RefSeqNP_873397.1. NC_002940.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SR4X-ray2.00A18-223[»]
ProteinModelPortalO06522.
SMRO06522. Positions 57-223.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1490844.
GenomeReviewsGene locus HD_0902 in contig AE017143_GR.
KEGGhdu:HD0902.
NMPDRfig|233412.1.peg.762.
PATRIC20178201. VBIHaeDuc133973_0743.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG495485.
OMAHREYFRF.
ProtClustDBCLSK2462536.

Enzyme and pathway databases

BioCycHDUC233412:HD_0902-MONOMER.

Family and domain databases

InterProIPR015957. CDtoxinA.
IPR003558. CDtoxinA/C.
IPR008997. Ricin_B-rel_lectin.
IPR000772. Ricin_B_lectin.
[Graphical view]
KOK11013.
PfamPF03498. CDtoxinA. 1 hit.
[Graphical view]
PIRSFPIRSF036516. CDT_A. 1 hit.
PRINTSPR01387. CDTOXINA.
SUPFAMSSF50370. RicinB_like. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDTA_HAEDU
AccessionPrimary (citable) accession number: O06522
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 1, 1997
Last modified: January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents