CDTA_HAEDU
ID CDTA_HAEDU Reviewed; 223 AA.
AC O06522;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Cytolethal distending toxin subunit A;
DE Short=CDT A;
DE Flags: Precursor;
GN Name=cdtA; OrderedLocusNames=HD_0902;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RX PubMed=9108104; DOI=10.1073/pnas.94.8.4056;
RA Cope L.D., Lumbley S., Latimer J.L., Klesney-Tait J., Stevens M.K.,
RA Johnson L.S., Purven M., Munson R.S. Jr., Lagergard T., Radolf J.D.,
RA Hansen E.J.;
RT "A diffusible cytotoxin of Haemophilus ducreyi.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4056-4061(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-223, FUNCTION, MUTAGENESIS OF
RP TRP-91; TRP-98; TRP-100 AND TYR-102, AND SUBUNIT.
RX PubMed=15164065; DOI=10.1038/nature02532;
RA Nesic D., Hsu Y., Stebbins C.E.;
RT "Assembly and function of a bacterial genotoxin.";
RL Nature 429:429-433(2004).
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 {ECO:0000269|PubMed:15164065}.
CC -!- SUBUNIT: Heterotrimer of 3 subunits, CdtA, CdtB and CdtC.
CC {ECO:0000269|PubMed:15164065}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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DR EMBL; U53215; AAB57725.1; -; Genomic_DNA.
DR EMBL; AE017143; AAP95786.1; -; Genomic_DNA.
DR RefSeq; WP_010944836.1; NC_002940.2.
DR PDB; 1SR4; X-ray; 2.00 A; A=18-223.
DR PDBsum; 1SR4; -.
DR AlphaFoldDB; O06522; -.
DR SMR; O06522; -.
DR STRING; 233412.HD_0902; -.
DR EnsemblBacteria; AAP95786; AAP95786; HD_0902.
DR KEGG; hdu:HD_0902; -.
DR eggNOG; ENOG50347HZ; Bacteria.
DR HOGENOM; CLU_1243172_0_0_6; -.
DR OMA; WLWGYTP; -.
DR EvolutionaryTrace; O06522; -.
DR Proteomes; UP000001022; 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 DisProt; DP03020; -.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lectin; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Toxin; Virulence.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..223
FT /note="Cytolethal distending toxin subunit A"
FT /id="PRO_0000013371"
FT DOMAIN 123..212
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 20..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..102
FT /note="Mediates binding to target cells"
FT /evidence="ECO:0000305"
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"
FT MUTAGEN 91
FT /note="W->G: Abolishes toxicity towards intact cells; when
FT associated with G-98; G-100 and G-102."
FT /evidence="ECO:0000269|PubMed:15164065"
FT MUTAGEN 98
FT /note="W->G: Abolishes toxicity towards intact cells; when
FT associated with G-91; G-100 and G-102."
FT /evidence="ECO:0000269|PubMed:15164065"
FT MUTAGEN 100
FT /note="W->G: Abolishes toxicity towards intact cells; when
FT associated with G-91; G-98 and G-102."
FT /evidence="ECO:0000269|PubMed:15164065"
FT MUTAGEN 102
FT /note="Y->G: Abolishes toxicity towards intact cells; when
FT associated with G-91; G-98 and G-100."
FT /evidence="ECO:0000269|PubMed:15164065"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1SR4"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1SR4"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1SR4"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1SR4"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1SR4"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1SR4"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1SR4"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1SR4"
SQ SEQUENCE 223 AA; 24664 MW; 5CA68F05958CD56D CRC64;
MKKFLPSLLL MGSVACSSNQ RMNDYSQPES QSDLAPKSST IQPQPQPLLS KTPSMSLNLL
SSSGPNRQVL PSEPSNFMTL MGQNGALLTV WALAKRNWLW AYPNIYSQDF GNIRNWKMEP
GKHREYFRFV NQSLGTCVEA YGNGLIHDIC SLDKLAQEFE LLPTDSGAVV IKSVSQGRCV
TYNPVSTTFY STVTLSVCDG ATEPSRDQTW YLAPPVLEAT AVN
