CDTB_ECOLX
ID CDTB_ECOLX Reviewed; 269 AA.
AC Q46669;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cytolethal distending toxin subunit B;
DE Short=CDT B;
DE AltName: Full=Deoxyribonuclease CdtB;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=cdtB;
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).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF HIS-154.
RX PubMed=11292766; DOI=10.1128/iai.69.5.3418-3422.2001;
RA Elwell C.A., Chao K., Patel K., Dreyfus L.A.;
RT "Escherichia coli CdtB mediates cytolethal distending toxin cell cycle
RT arrest.";
RL Infect. Immun. 69:3418-3422(2001).
RN [3]
RP MUTAGENESIS OF HIS-154; ASP-229; ASP-260 AND HIS-261.
RX PubMed=10972814; DOI=10.1046/j.1365-2958.2000.02070.x;
RA Elwell C.A., Dreyfus L.A.;
RT "DNase I homologous residues in CdtB are critical for cytolethal distending
RT toxin-mediated cell cycle arrest.";
RL Mol. Microbiol. 37:952-963(2000).
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF THE NUCLEAR LOCALIZATION
RP SIGNAL.
RX PubMed=15056215; DOI=10.1111/j.1462-5822.2004.00373.x;
RA McSweeney L.A., Dreyfus L.A.;
RT "Nuclear localization of the Escherichia coli cytolethal distending toxin
RT CdtB subunit.";
RL Cell. Microbiol. 6:447-458(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 19-269.
RX PubMed=16809347; DOI=10.1074/jbc.m603727200;
RA Hontz J.S., Villar-Lecumberri M.T., Potter B.M., Yoder M.D., Dreyfus L.A.,
RA Laity J.H.;
RT "Differences in crystal and solution structures of the cytolethal
RT distending toxin B subunit: Relevance to nuclear translocation and
RT functional activation.";
RL J. Biol. Chem. 281:25365-25372(2006).
CC -!- FUNCTION: Part of the tripartite complex that is required for the CDT
CC activity. CdtB exhibits a DNA-nicking endonuclease activity, and very
CC probably causes DNA damage in intoxicated cells. This damage induces
CC G2/M cell cycle arrest, chromatin fragmentation, cell distention and
CC nucleus enlargement. {ECO:0000269|PubMed:11292766}.
CC -!- SUBUNIT: Heterotrimer of 3 subunits, CdtA, CdtB and CdtC.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15056215}.
CC Note=Localized to the nucleus of the infected cells.
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; AAA18786.1; -; Unassigned_DNA.
DR PIR; I69095; I69095.
DR PDB; 2F1N; X-ray; 1.73 A; A=19-269.
DR PDBsum; 2F1N; -.
DR AlphaFoldDB; Q46669; -.
DR BMRB; Q46669; -.
DR SMR; Q46669; -.
DR TCDB; 1.C.98.1.1; the cytolethal distending toxin (cdt) family.
DR EvolutionaryTrace; Q46669; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd09081; CdtB; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR003539; CD_toxinB.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR PIRSF; PIRSF018539; CDT_B; 1.
DR PRINTS; PR01388; CDTOXINB.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Secreted; Signal; Toxin;
KW Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..269
FT /note="Cytolethal distending toxin subunit B"
FT /id="PRO_0000013373"
FT MOTIF 195..210
FT /note="Nuclear localization signal"
FT MUTAGEN 154
FT /note="H->A: When the mutant protein is introduced in HeLa
FT cells, it does not result in cell cycle arrest. Devoid of
FT DNA-nicking/DNase activity."
FT /evidence="ECO:0000269|PubMed:10972814,
FT ECO:0000269|PubMed:11292766"
FT MUTAGEN 229
FT /note="D->A: Loss of DNase activity, no cellular
FT distension, no G2/M cell cycle arrest."
FT /evidence="ECO:0000269|PubMed:10972814"
FT MUTAGEN 260
FT /note="D->R: Loss of DNase activity, no cellular
FT distension, no G2/M cell cycle arrest."
FT /evidence="ECO:0000269|PubMed:10972814"
FT MUTAGEN 261
FT /note="H->A: Loss of DNase activity, no cellular
FT distension, no G2/M cell cycle arrest."
FT /evidence="ECO:0000269|PubMed:10972814"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:2F1N"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:2F1N"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2F1N"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:2F1N"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:2F1N"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:2F1N"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:2F1N"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:2F1N"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2F1N"
SQ SEQUENCE 269 AA; 29529 MW; 958B09BD6C73EBB5 CRC64;
MKKYIISLIV FLSFYAQADL TDFRVATWNL QGASATTESK WNINVRQLIS GENAVDILAV
QEAGSPPSTA VDTGTLIPSP GIPVRELIWN LSTNSRPQQV YIYFSAVDAL GGRVNLALVS
NRRADEVFVL SPVRQGGRPL LGIRIGNDAF FTAHAIAMRN NDAPALVEEV YNFFRDSRDP
VHQALNWMIL GDFNREPADL EMNLTVPVRR ASEIISPAAA TQTSQRTLDY AVAGNSVAFR
PSPLQAGIVY GARRTQISSD HFPVGVSRR
