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O87120 (CDTA_AGGAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytolethal distending toxin subunit A
Short name=CDT A
Gene names
Name:cdtA
OrganismAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifier714 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Aggregatibacter

Protein attributes

Sequence length222 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. Ref.5

Subunit structure

Heterotrimer of 3 subunits, CdtA, CdtB and CdtC. May form higher oligomers. Ref.4 Ref.5

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
Direct protein sequencing
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 – 222207Cytolethal distending toxin subunit A
PRO_0000013368

Regions

Domain122 – 21190Ricin B-type lectin
Region90 – 10112Mediates binding to target cells By similarity

Amino acid modifications

Lipidation161N-palmitoyl cysteine Probable
Lipidation161S-diacylglycerol cysteine Probable

Secondary structure

1 .................................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O87120 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D8267171A2EA4774

FASTA22224,514
        10         20         30         40         50         60 
MKKFLPGLLL MGLVACSSNQ RMSDYSQPES QSDLAPKSST TQFQPQPLLS KASSMPLNLL 

        70         80         90        100        110        120 
SSSKNGQVSP SEPSNFMTLM GQNGALLTVW ALAKRNWLWA YPNIYSQDFG NIRNWKIEPG 

       130        140        150        160        170        180 
KHREYFRFVN QSLGTCIEAY GNGLIHDTCS LDKLAQEFEL LPTDSGAVVI KSVSQGRCVT 

       190        200        210        220 
YNPVSPTYYS TVTLSTCDGA TEPLRDQTWY LAPPVLEATA VN

« Hide

References

[1]"The cell cycle-specific growth-inhibitory factor produced by Actinobacillus actinomycetemcomitans is a cytolethal distending toxin."
Sugai M., Kawamoto T., Peres S.Y., Ueno Y., Komatsuzawa H., Fujiwara T., Kurihara H., Suginaka H., Oswald E.
Infect. Immun. 66:5008-5019(1998) [PubMed: 9746611] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43718 / FDC Y4 / Serotype b.
[2]"Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitans."
Mayer M.P., Bueno L.C., Hansen E.J., DiRienzo J.M.
Infect. Immun. 67:1227-1237(1999) [PubMed: 10024565] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43718 / FDC Y4 / Serotype b.
[3]"Expression of the cytolethal distending toxin (Cdt) operon in Actinobacillus actinomycetemcomitans: evidence that the CdtB protein is responsible for G2 arrest of the cell cycle in human T cells."
Shenker B.J., Hoffmaster R.H., McKay T.L., Demuth D.R.
J. Immunol. 165:2612-2618(2000) [PubMed: 10946289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 652.
[4]"Reconstitution and purification of cytolethal distending toxin of Actinobacillus actinomycetemcomitans."
Saiki K., Konishi K., Gomi T., Nishihara T., Yoshikawa M.
Microbiol. Immunol. 45:497-506(2001) [PubMed: 11497226] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-57, SUBUNIT.
Strain: ATCC 29522 / NCTC 10979 / Serotype b.
[5]"Variation of loop sequence alters stability of cytolethal distending toxin (CDT): crystal structure of CDT from Actinobacillus actinomycetemcomitans."
Yamada T., Komoto J., Saiki K., Konishi K., Takusagawa F.
Protein Sci. 15:362-372(2006) [PubMed: 16434747] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB011405 Genomic DNA. Translation: BAA33485.1.
AF006830 Genomic DNA. Translation: AAC70897.1.
AF102554 Genomic DNA. Translation: AAG09113.1.
AB017807 Genomic DNA. Translation: BAA35116.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F2FX-ray2.40A/D1-222[»]
ProteinModelPortalO87120.
SMRO87120. Positions 70-222.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR015957. CDtoxinA.
IPR003558. CDtoxinA/C.
IPR008997. Ricin_B-rel_lectin.
IPR000772. Ricin_B_lectin.
[Graphical view]
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_AGGAC
AccessionPrimary (citable) accession number: O87120
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1998
Last modified: May 31, 2011
This is version 70 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