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Protein

Cytolethal distending toxin subunit A

Gene

cdtA

Organism
Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

CDTs are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Cytolethal distending toxin subunit A
Short name:
CDT A
Gene namesi
Name:cdtA
OrganismiAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifieri714 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515PROSITE-ProRule annotationAdd
BLAST
Chaini16 – 222207Cytolethal distending toxin subunit APRO_0000013368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi16 – 161N-palmitoyl cysteineCurated
Lipidationi16 – 161S-diacylglycerol cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Heterotrimer of 3 subunits, CdtA, CdtB and CdtC. May form higher oligomers.2 Publications

Protein-protein interaction databases

STRINGi694569.D7S_2348.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi73 – 753Combined sources
Beta strandi77 – 815Combined sources
Beta strandi84 – 896Combined sources
Beta strandi97 – 1026Combined sources
Helixi103 – 1053Combined sources
Helixi107 – 1137Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi126 – 1305Combined sources
Turni131 – 1333Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi143 – 1475Combined sources
Helixi154 – 1563Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi168 – 1725Combined sources
Turni173 – 1753Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi186 – 19510Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi218 – 2203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F2FX-ray2.40A/D1-222[»]
ProteinModelPortaliO87120.
SMRiO87120. Positions 70-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO87120.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 21190Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 10112Mediates binding to target cellsBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106BMH. Bacteria.
ENOG410Y0HS. LUCA.

Family and domain databases

InterProiIPR015957. CDtoxinA.
IPR003558. CDtoxinA/C.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF03498. CDtoxinA. 1 hit.
[Graphical view]
PIRSFiPIRSF036516. CDT_A. 1 hit.
PRINTSiPR01387. CDTOXINA.
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O87120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFLPGLLL MGLVACSSNQ RMSDYSQPES QSDLAPKSST TQFQPQPLLS
60 70 80 90 100
KASSMPLNLL SSSKNGQVSP SEPSNFMTLM GQNGALLTVW ALAKRNWLWA
110 120 130 140 150
YPNIYSQDFG NIRNWKIEPG KHREYFRFVN QSLGTCIEAY GNGLIHDTCS
160 170 180 190 200
LDKLAQEFEL LPTDSGAVVI KSVSQGRCVT YNPVSPTYYS TVTLSTCDGA
210 220
TEPLRDQTWY LAPPVLEATA VN
Length:222
Mass (Da):24,514
Last modified:November 1, 1998 - v1
Checksum:iD8267171A2EA4774
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011405 Genomic DNA. Translation: BAA33485.1.
AF006830 Genomic DNA. Translation: AAC70897.1.
AF102554 Genomic DNA. Translation: AAG09113.1.
AB017807 Genomic DNA. Translation: BAA35116.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F2FX-ray2.40A/D1-222[»]
ProteinModelPortaliO87120.
SMRiO87120. Positions 70-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi694569.D7S_2348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4106BMH. Bacteria.
ENOG410Y0HS. LUCA.

Miscellaneous databases

EvolutionaryTraceiO87120.

Family and domain databases

InterProiIPR015957. CDtoxinA.
IPR003558. CDtoxinA/C.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF03498. CDtoxinA. 1 hit.
[Graphical view]
PIRSFiPIRSF036516. CDT_A. 1 hit.
PRINTSiPR01387. CDTOXINA.
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION, SUBUNIT.

Entry informationi

Entry nameiCDTA_AGGAC
AccessioniPrimary (citable) accession number: O87120
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1998
Last modified: December 9, 2015
This is version 89 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, Direct protein sequencing

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.