ID   CDTC_ECOLX              Reviewed;         181 AA.
AC   Q46670;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cytolethal distending toxin subunit C;
DE            Short=CDT C;
DE   Flags: Precursor;
GN   Name=cdtC;
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: Part of the tripartite complex that is required for the CDT
CC       activity. CdtC, along with CdtA, probably forms a heterodimeric subunit
CC       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; AAA18787.1; -; Unassigned_DNA.
DR   PIR; I69096; I69096.
DR   AlphaFoldDB; Q46670; -.
DR   SMR; Q46670; -.
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; IPR003558; CDtoxinA/C.
DR   InterPro; IPR003559; CDtoxinC.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF03498; CDtoxinA; 1.
DR   PRINTS; PR01389; CDTOXINC.
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..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..181
FT                   /note="Cytolethal distending toxin subunit C"
FT                   /id="PRO_0000013375"
FT   DOMAIN          79..181
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   181 AA;  19881 MW;  D89EB3E4A2744AC0 CRC64;
     MKKLAIVFTM LLIAGCSSSQ DSANNQIDEL GKENNSLFTF RNIQSGLMIH NGLHQHGRET
     IGWEIVPVKT PEEALVTDQS GWIMIRTPNT DQCLGTPDGR NLLKMTCNST AKKTLFSLIP
     STTGAVQIKS VLSGLCFLDS KNSGLSFETG KCIADFKKPF EVVPQSHLWM LNPLNTESPI
     I