CDTA_CAMJE
ID CDTA_CAMJE Reviewed; 268 AA.
AC Q0PC56; Q46100;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cytolethal distending toxin subunit A;
DE Short=CDT A;
DE Flags: Precursor;
GN Name=cdtA; OrderedLocusNames=Cj0079c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CH5;
RA Scott D.A., McVeigh A.L., Pratt C., Lee L., Michielutti R.E., Kinsella N.,
RA Trust T.J., Guerry P.;
RT "Coordinate regulation of virulence factors of Campylobacter spp. by bile
RT salts.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: CDTs are cytotoxins which induce cell distension, growth
CC arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in
CC HeLa cells. {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of 3 subunits, CdtA, CdtB and CdtC.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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DR EMBL; AF038283; AAF16678.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34252.1; -; Genomic_DNA.
DR PIR; A81424; A81424.
DR RefSeq; WP_002852021.1; NC_002163.1.
DR RefSeq; YP_002343541.1; NC_002163.1.
DR AlphaFoldDB; Q0PC56; -.
DR SMR; Q0PC56; -.
DR STRING; 192222.Cj0079c; -.
DR PaxDb; Q0PC56; -.
DR PRIDE; Q0PC56; -.
DR EnsemblBacteria; CAL34252; CAL34252; Cj0079c.
DR GeneID; 904406; -.
DR KEGG; cje:Cj0079c; -.
DR PATRIC; fig|192222.6.peg.78; -.
DR eggNOG; ENOG50347HZ; Bacteria.
DR HOGENOM; CLU_090932_0_0_7; -.
DR OMA; WGYSARD; -.
DR PHI-base; PHI:7848; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR015957; CDtoxinA.
DR InterPro; IPR003558; CDtoxinA/C.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF03498; CDtoxinA; 1.
DR PIRSF; PIRSF036516; CDT_A; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Lectin; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Toxin; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..268
FT /note="Cytolethal distending toxin subunit A"
FT /id="PRO_0000013369"
FT DOMAIN 112..252
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 129..140
FT /note="Mediates binding to target cells"
FT /evidence="ECO:0000250"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 29919 MW; 8E130277E8499A74 CRC64;
MQKIIVFILC CFMTFFLYAC SSKFENVNPL GRSFGEFEDT DPLKLGLEPT FPTNQEIPSL
ISGADLVPIT PITPPLTRTS NSANNNAANG INPRFKDEAF NDVLIFENRP AVSDFLTILG
PSGAALTVWA LAQGNWIWGY TLIDSKGFGD ARVWQLLLYP NDFAMIKNAK TNTCLNAYGN
GIVHYPCDAS NHAQMWKLIP MSNTAVQIKN LGNGKCIQAP ITNLYGDFHK VFKIFTVECA
KKDNFDQQWF LTTPPFTAKP LYRQGEVR