ID   DTXH_CORBE              Reviewed;         560 AA.
AC   P00589;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Diphtheria toxin homolog CRM228;
DE   Contains:
DE     RecName: Full=Diphtheria toxin homolog CRM228 fragment A;
DE   Contains:
DE     RecName: Full=Diphtheria toxin homolog CRM228 fragment B;
DE   Flags: Precursor;
OS   Corynephage beta.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus; unclassified Lambdavirus.
OX   NCBI_TaxID=10703;
OH   NCBI_TaxID=1717; Corynebacterium diphtheriae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6348945; DOI=10.1126/science.6348945;
RA   Kaczorek M., Delpeyroux F., Chenciner N., Streeck R.E., Murphy J.R.,
RA   Boquet P., Tiollais P.;
RT   "Nucleotide sequence and expression of the diphtheria tox228 gene in
RT   Escherichia coli.";
RL   Science 221:855-858(1983).
CC   -!- MISCELLANEOUS: This diphtheria toxin homolog is a nontoxic cross-
CC       reacting material (CRM) produced by a strain of corynephage beta that
CC       had undergone N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis. This
CC       treatment induces guanine-adenine transitions in the DNA; the
CC       differences from the wild-type sequence at positions 104, 187, 222, 456
CC       and 532 can be explained by such mutations. Either of the first 2
CC       mutations will completely abolish all ADP-ribosylating activity of
CC       fragment A. The last 2 mutations may be responsible for the reduced
CC       receptor-binding capacity of this protein.
CC   -!- MISCELLANEOUS: In wild-type active diphtheria toxin, fragment A
CC       catalyzes the ADP-ribosylation of elongation factor 2 and blocks
CC       protein synthesis in eukaryotic cells; fragment B binds to the receptor
CC       protein and is necessary for the movement of fragment A into the cell.
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DR   EMBL; K01723; AAA32183.1; -; Genomic_DNA.
DR   BMRB; P00589; -.
DR   SMR; P00589; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0047286; F:NAD+-diphthamide ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:InterPro.
DR   Gene3D; 2.60.40.700; -; 1.
DR   InterPro; IPR036799; Diphtheria_tox_rcpt-bd_dom_sf.
DR   InterPro; IPR036801; Diphtheria_tox_transloc_sf.
DR   InterPro; IPR000512; Diphtheria_toxin.
DR   InterPro; IPR022406; Diphtheria_toxin_catalytic_dom.
DR   InterPro; IPR022404; Diphtheria_toxin_rcpt-bd_dom.
DR   InterPro; IPR022405; Diphtheria_toxin_translocation.
DR   Pfam; PF02763; Diphtheria_C; 1.
DR   Pfam; PF01324; Diphtheria_R; 1.
DR   Pfam; PF02764; Diphtheria_T; 1.
DR   PIRSF; PIRSF000490; Diphtheria_toxin; 1.
DR   PRINTS; PR00769; DPTHRIATOXIN.
DR   SUPFAM; SSF49380; SSF49380; 1.
DR   SUPFAM; SSF56845; SSF56845; 1.
PE   4: Predicted;
KW   Cleavage on pair of basic residues; Disulfide bond; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..218
FT                   /note="Diphtheria toxin homolog CRM228 fragment A"
FT                   /id="PRO_0000019349"
FT   CHAIN           219..560
FT                   /note="Diphtheria toxin homolog CRM228 fragment B"
FT                   /id="PRO_0000019350"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        486..496
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   560 AA;  60921 MW;  BDE723239CE4F2C1 CRC64;
     MSRKLFASIL IGALLGIGAP PSAHAGADDV VDSSKSFVME NFSSYHGTKP GYVDSIQKGI
     QKPKSGTQGN YDDDWKGFYS TDNKYDAAGY SVDNENPLSG KAGDVVKVTY PGLTKVLALK
     VDNAETIKKE LGLSLTEPLM EQVGTEEFIK RFGDGASRVV LSLPFAEGSS SVEYINNWEQ
     AKALSVKLEI NFETRGKRGQ DAMYEYMAQA CAGNRVRRSV GGSLSCINLD WDVIRDKTKT
     KIESLKEHGP IKNKMSESPN KTVSEEKAKQ YLEEFHQTAL EHPELSELKT VTGTNRVFAG
     ANYAAWAVNV AQVIDSETAD NLEKTTAALS ILPGIGSVMG IADGAVHHNT EEIVAQSIAL
     SSLMVAQAIP LVGELVDIGF AAYNFVESII NLFQVVHNSY NRSAYSPGHK TQPFLHDGYA
     VSWNTVEDSI IRTGFQGESG HDIKITAENT PLPIASVLLP TIPGKLDVNK SKTHISVNGR
     KIRMRCRAID GDVTFCRPKS PVYVGNGVHA NLHVAFHRSS SEKIHSNEIS SDSIGVLGYQ
     KTVDHTKVNS KLSLFFEIKS