CDTA_AGGAC
ID CDTA_AGGAC Reviewed; 222 AA.
AC O87120;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Cytolethal distending toxin subunit A;
DE Short=CDT A;
DE Flags: Precursor;
GN Name=cdtA;
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RX PubMed=9746611; DOI=10.1128/iai.66.10.5008-5019.1998;
RA Sugai M., Kawamoto T., Peres S.Y., Ueno Y., Komatsuzawa H., Fujiwara T.,
RA Kurihara H., Suginaka H., Oswald E.;
RT "The cell cycle-specific growth-inhibitory factor produced by
RT Actinobacillus actinomycetemcomitans is a cytolethal distending toxin.";
RL Infect. Immun. 66:5008-5019(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RX PubMed=10024565; DOI=10.1128/iai.67.3.1227-1237.1999;
RA Mayer M.P., Bueno L.C., Hansen E.J., DiRienzo J.M.;
RT "Identification of a cytolethal distending toxin gene locus and features of
RT a virulence-associated region in Actinobacillus actinomycetemcomitans.";
RL Infect. Immun. 67:1227-1237(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=652;
RX PubMed=10946289; DOI=10.4049/jimmunol.165.5.2612;
RA Shenker B.J., Hoffmaster R.H., McKay T.L., Demuth D.R.;
RT "Expression of the cytolethal distending toxin (Cdt) operon in
RT Actinobacillus actinomycetemcomitans: evidence that the CdtB protein is
RT responsible for G2 arrest of the cell cycle in human T cells.";
RL J. Immunol. 165:2612-2618(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-57, AND SUBUNIT.
RC STRAIN=ATCC 29522 / NCTC 10979 / Serotype b;
RX PubMed=11497226; DOI=10.1111/j.1348-0421.2001.tb02650.x;
RA Saiki K., Konishi K., Gomi T., Nishihara T., Yoshikawa M.;
RT "Reconstitution and purification of cytolethal distending toxin of
RT Actinobacillus actinomycetemcomitans.";
RL Microbiol. Immunol. 45:497-506(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=16434747; DOI=10.1110/ps.051790506;
RA Yamada T., Komoto J., Saiki K., Konishi K., Takusagawa F.;
RT "Variation of loop sequence alters stability of cytolethal distending toxin
RT (CDT): crystal structure of CDT from Actinobacillus
RT actinomycetemcomitans.";
RL Protein Sci. 15:362-372(2006).
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. {ECO:0000269|PubMed:16434747}.
CC -!- SUBUNIT: Heterotrimer of 3 subunits, CdtA, CdtB and CdtC. May form
CC higher oligomers. {ECO:0000269|PubMed:11497226,
CC ECO:0000269|PubMed:16434747}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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DR EMBL; AB011405; BAA33485.1; -; Genomic_DNA.
DR EMBL; AF006830; AAC70897.1; -; Genomic_DNA.
DR EMBL; AF102554; AAG09113.1; -; Genomic_DNA.
DR EMBL; AB017807; BAA35116.1; -; Genomic_DNA.
DR RefSeq; WP_005540930.1; NZ_VSEW01000012.1.
DR PDB; 2F2F; X-ray; 2.40 A; A/D=1-222.
DR PDBsum; 2F2F; -.
DR AlphaFoldDB; O87120; -.
DR SMR; O87120; -.
DR STRING; 714.ACT75_10585; -.
DR eggNOG; ENOG50347HZ; Bacteria.
DR OMA; WLWGYTP; -.
DR EvolutionaryTrace; O87120; -.
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; DP01002; -.
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; Direct protein sequencing; Lectin;
KW Lipoprotein; Membrane; Palmitate; Signal; Toxin; Virulence.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..222
FT /note="Cytolethal distending toxin subunit A"
FT /id="PRO_0000013368"
FT DOMAIN 122..211
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 22..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..101
FT /note="Mediates binding to target cells"
FT /evidence="ECO:0000250"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2F2F"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2F2F"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2F2F"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2F2F"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2F2F"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2F2F"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2F2F"
SQ SEQUENCE 222 AA; 24514 MW; D8267171A2EA4774 CRC64;
MKKFLPGLLL MGLVACSSNQ RMSDYSQPES QSDLAPKSST TQFQPQPLLS KASSMPLNLL
SSSKNGQVSP SEPSNFMTLM GQNGALLTVW ALAKRNWLWA YPNIYSQDFG NIRNWKIEPG
KHREYFRFVN QSLGTCIEAY GNGLIHDTCS LDKLAQEFEL LPTDSGAVVI KSVSQGRCVT
YNPVSPTYYS TVTLSTCDGA TEPLRDQTWY LAPPVLEATA VN
