CDTB_SALTI
ID CDTB_SALTI Reviewed; 269 AA.
AC Q8Z6A7; Q7CAE0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Cytolethal distending toxin subunit B homolog;
DE Short=CDT B;
DE AltName: Full=Deoxyribonuclease CdtB;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=cdtB; OrderedLocusNames=STY1886, t1111;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3]
RP CHARACTERIZATION OF THE TOXIC ACTIVITY, AND MUTAGENESIS OF HIS-160 AND
RP ASP-195.
RC STRAIN=ISP2825;
RX PubMed=15070766; DOI=10.1073/pnas.0400932101;
RA Haghjoo E., Galan J.E.;
RT "Salmonella typhi encodes a functional cytolethal distending toxin that is
RT delivered into host cells by a bacterial-internalization pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4614-4619(2004).
CC -!- FUNCTION: Produces a CDT (cytolethal distending toxin) activity, which
CC causes DNA damage in intoxicated cells. This damage induces G2/M cell
CC cycle arrest, chromatin fragmentation, cell distention and nucleus
CC enlargement.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Localized to the nucleus of
CC infected cells.
CC -!- INDUCTION: Expressed only on infection of host cells.
CC -!- MISCELLANEOUS: Unlike other pathogens possessing a CDT activity,
CC S.typhi does not encode CdtA and CdtC (that form a heterodimeric
CC subunit), which are required for the delivery of CdtB. It means that
CC the CDT activity of S.typhi is strictly dependent on CdtB. Both CDT
CC activity and expression of CdtB require S.typhi internalization into
CC host cells.
CC -!- MISCELLANEOUS: S.typhi is the only Salmonella serovar that encodes
CC cdtB.
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DR EMBL; AL513382; CAD02120.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68774.1; -; Genomic_DNA.
DR RefSeq; NP_456275.1; NC_003198.1.
DR RefSeq; WP_001529135.1; NZ_WSUR01000044.1.
DR PDB; 4K6L; X-ray; 2.39 A; F=23-269.
DR PDB; 6VX4; EM; 3.12 A; F=23-269.
DR PDBsum; 4K6L; -.
DR PDBsum; 6VX4; -.
DR AlphaFoldDB; Q8Z6A7; -.
DR SMR; Q8Z6A7; -.
DR DIP; DIP-60315N; -.
DR IntAct; Q8Z6A7; 3.
DR STRING; 220341.16502954; -.
DR EnsemblBacteria; AAO68774; AAO68774; t1111.
DR KEGG; stt:t1111; -.
DR KEGG; sty:STY1886; -.
DR PATRIC; fig|220341.7.peg.1901; -.
DR eggNOG; COG3021; Bacteria.
DR HOGENOM; CLU_091266_0_0_6; -.
DR OMA; IEEYTWN; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Secreted; Signal; Toxin;
KW Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..269
FT /note="Cytolethal distending toxin subunit B homolog"
FT /id="PRO_0000013374"
FT MUTAGEN 160
FT /note="H->Q: Abolishes cytotoxic activity."
FT /evidence="ECO:0000269|PubMed:15070766"
FT MUTAGEN 195
FT /note="D->S: Abolishes cytotoxic activity."
FT /evidence="ECO:0000269|PubMed:15070766"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6VX4"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6VX4"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6VX4"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6VX4"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:6VX4"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:6VX4"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6VX4"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6VX4"
SQ SEQUENCE 269 AA; 29560 MW; C00038DFDC03C2BA CRC64;
MKKPVFFLLT MIICSYISFA CANISDYKVM TWNLQGSSAS TESKWNVNVR QLLSGTAGVD
ILMVQEAGAV PTSAVPTGRH IQPFGVGIPI DEYTWNLGTT SRQDIRYIYH SAIDVGARRV
NLAIVSRQRA DNVYVLRPTT VASRPVIGIG LGNDVFLTAH ALASGGPDAA AIVRVTINFF
RQPQMRHLSW FLAGDFNRSP DRLENDLMTE HLERVVAVLA PTEPTQIGGG ILDYGVIVDR
APYSQRVEAL RNPQLASDHY PVAFLARSC
