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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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15PROSITE-ProRule annotationAdd BLAST15
ChainiPRO_000001336816 – 222Cytolethal distending toxin subunit AAdd BLAST207

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi16N-palmitoyl cysteineCurated1
Lipidationi16S-diacylglycerol cysteineCurated1

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

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi73 – 75Combined sources3
Beta strandi77 – 81Combined sources5
Beta strandi84 – 89Combined sources6
Beta strandi97 – 102Combined sources6
Helixi103 – 105Combined sources3
Helixi107 – 113Combined sources7
Beta strandi115 – 119Combined sources5
Beta strandi126 – 130Combined sources5
Turni131 – 133Combined sources3
Beta strandi136 – 140Combined sources5
Beta strandi143 – 147Combined sources5
Helixi154 – 156Combined sources3
Beta strandi158 – 163Combined sources6
Beta strandi168 – 172Combined sources5
Turni173 – 175Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi186 – 195Combined sources10
Beta strandi208 – 212Combined sources5
Beta strandi218 – 220Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO87120.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini122 – 211Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni90 – 101Mediates binding to target cellsBy similarityAdd BLAST12

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.
RefSeqiWP_005540930.1. NZ_CP016553.1.

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.
RefSeqiWP_005540930.1. NZ_CP016553.1.

3D structure databases

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

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: November 2, 2016
This is version 92 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.