ID   CDTA_ECOLX              Reviewed;         258 AA.
AC   Q46668;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Cytolethal distending toxin subunit A;
DE            Short=CDT A;
DE   Flags: Precursor;
GN   Name=cdtA;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O128:H- / 9142-88 / EPEC;
RX   PubMed=8112838; DOI=10.1128/iai.62.3.1046-1051.1994;
RA   Pickett C.L., Cottle D.L., Pesci E.C., Bikah G.;
RT   "Cloning, sequencing, and expression of the Escherichia coli cytolethal
RT   distending toxin genes.";
RL   Infect. Immun. 62:1046-1051(1994).
CC   -!- FUNCTION: CDTs are cytotoxins which induce host cell distension, growth
CC       arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in
CC       HeLa cells. CdtA, along with CdtC, probably forms a heterodimeric
CC       subunit required for the delivery of CdtB.
CC   -!- SUBUNIT: Heterotrimer of 3 subunits, CdtA, CdtB and CdtC.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: The operon of the strain O128:H- / 9142-88 / EPEC is
CC       referred to as cdt type II (CDT-II).
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DR   EMBL; U04208; AAA18785.1; -; Unassigned_DNA.
DR   PIR; I54627; I54627.
DR   AlphaFoldDB; Q46668; -.
DR   SMR; Q46668; -.
DR   TCDB; 1.C.98.1.1; the cytolethal distending toxin (cdt) family.
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   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   PRINTS; PR01387; CDTOXINA.
DR   SUPFAM; SSF50370; SSF50370; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..258
FT                   /note="Cytolethal distending toxin subunit A"
FT                   /id="PRO_0000013370"
FT   DOMAIN          125..223
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          40..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..104
FT                   /note="Mediates binding to target cells"
FT                   /evidence="ECO:0000250"
FT   REGION          236..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  27712 MW;  23A31F3AFD4D2F35 CRC64;
     MANKRTPIFI AGILIPILLN GCSSGKNKAY LDPKVFPPQV EGGPTVPSPD EPGLPLPGPG
     PALPTNGAIP IPEPGTAPAV SLMNMDGSVL TMWSRGAGSS LWAYYIGDSN SFGELRNWQI
     MPGTRPNTIQ FRNVDVGTCM TSFPGFKGGV QLSTAPCKFG PERFDFQPMA TRNGNYQLKS
     LSTGLCIRAN FLGRTPSSPY ATTLTMERCP SSGEKNFEFM WSISEPLRPA LATIAKPEIR
     PFPPQPIEPD EHSTGGEQ