ID   CDTA_CAMJJ              Reviewed;         268 AA.
AC   A1VXG4; Q46100;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Cytolethal distending toxin subunit A;
DE            Short=CDT A;
DE   Flags: Precursor;
GN   Name=cdtA; OrderedLocusNames=CJJ81176_0116;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8675309; DOI=10.1128/iai.64.6.2070-2078.1996;
RA   Pickett C.L., Pesci E.C., Cottle D.L., Russell G., Erdem A.N., Zeytin H.;
RT   "Prevalence of cytolethal distending toxin production in Campylobacter
RT   jejuni and relatedness of Campylobacter sp. cdtB gene.";
RL   Infect. Immun. 64:2070-2078(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SUBUNIT: Heterotrimer of 3 subunits, CdtA, CdtB and CdtC.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
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DR   EMBL; U51121; AAB06707.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ71960.1; -; Genomic_DNA.
DR   RefSeq; WP_002852021.1; NC_008787.1.
DR   AlphaFoldDB; A1VXG4; -.
DR   SMR; A1VXG4; -.
DR   STRING; 354242.CJJ81176_0116; -.
DR   EnsemblBacteria; EAQ71960; EAQ71960; CJJ81176_0116.
DR   KEGG; cjj:CJJ81176_0116; -.
DR   eggNOG; ENOG50347HZ; Bacteria.
DR   HOGENOM; CLU_090932_0_0_7; -.
DR   OMA; WGYSARD; -.
DR   Proteomes; UP000000646; 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; Signal;
KW   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_0000281897"
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