CRAX_BACCE
ID CRAX_BACCE Reviewed; 476 AA.
AC Q4MV79;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Putative ADP-ribosyltransferase Certhrax;
DE EC=2.4.2.-;
DE AltName: Full=Toxin Certhrax;
GN ORFNames=BCE_G9241_pBC218_0027;
OS Bacillus cereus.
OG Plasmid pBC218.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G9241;
RX PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J.,
RA Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T.,
RA Fraser C.M.;
RT "Identification of anthrax toxin genes in a Bacillus cereus associated with
RT an illness resembling inhalation anthrax.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN [2]
RP FUNCTION AS A TOXIN, EXPRESSION IN YEAST, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLN-429 AND GLU-431.
RC STRAIN=G9241;
RX PubMed=21170356; DOI=10.1371/journal.pcbi.1001029;
RA Fieldhouse R.J., Turgeon Z., White D., Merrill A.R.;
RT "Cholera- and anthrax-like toxins are among several new ADP-
RT ribosyltransferases.";
RL PLoS Comput. Biol. 6:E1001029-E1001029(2010).
CC -!- FUNCTION: A probable mono(ADP-ribosyl)transferase; it is not known
CC which residue is targeted for ADP-ribosylation. Upon expression in
CC yeast cells causes cell death. {ECO:0000269|PubMed:21170356}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; AAEK01000004; EAL15945.1; -; Genomic_DNA.
DR PDB; 4FK7; X-ray; 1.78 A; A=242-469.
DR PDB; 4FXQ; X-ray; 1.96 A; A/B=18-471.
DR PDB; 4GF1; X-ray; 2.25 A; A/B=18-471.
DR PDBsum; 4FK7; -.
DR PDBsum; 4FXQ; -.
DR PDBsum; 4GF1; -.
DR AlphaFoldDB; Q4MV79; -.
DR SMR; Q4MV79; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR003540; ADP-ribosyltransferase.
DR InterPro; IPR003541; Anthrax_toxin_lethal/edema.
DR InterPro; IPR014781; Anthrax_toxin_lethal/edema_N/C.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR Pfam; PF03496; ADPrib_exo_Tox; 1.
DR Pfam; PF07737; ATLF; 1.
DR PRINTS; PR01392; ANTHRAXTOXNA.
DR PROSITE; PS51995; ATLF; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; NAD; Nucleotide-binding;
KW Nucleotidyltransferase; Plasmid; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..476
FT /note="Putative ADP-ribosyltransferase Certhrax"
FT /id="PRO_0000410943"
FT DOMAIN 2..226
FT /note="ATLF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01339"
FT DOMAIN 242..470
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 398
FT /evidence="ECO:0000255"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 280..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 341..344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 382..384
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 398
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 431
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 429..431
FT /note="QYE->AYA: Restores 60% growth in yeast."
FT MUTAGEN 429
FT /note="Q->A: Restores 10% growth in yeast."
FT /evidence="ECO:0000269|PubMed:21170356"
FT MUTAGEN 431
FT /note="E->A: Restores 15% growth in yeast."
FT /evidence="ECO:0000269|PubMed:21170356"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:4FXQ"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 187..202
FT /evidence="ECO:0007829|PDB:4FXQ"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 228..242
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:4FK7"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:4FK7"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:4FXQ"
FT HELIX 313..329
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4GF1"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4FK7"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4FK7"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:4FK7"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:4GF1"
FT STRAND 460..468
FT /evidence="ECO:0007829|PDB:4FK7"
SQ SEQUENCE 476 AA; 55350 MW; 6244734785B0E007 CRC64;
MKEIIRNLVR LDVRSDVDEN SKKTQELVEK LPHEVLELYK NVGGEIYITD KRLTQHEELS
DSSHKDMFIV SSEGKSFPLR EHFVFAKGGK EPSLIIHAED YASHLSSVEV YYELGKAIIR
DTFPLNQKEL GNPKFINAIN EVNQQKEGKG VNAKADEDGR DLLFGKELKK NLEHGQLVDL
DLISGNLSEF QHVFAKSFAL YYEPHYKEAL KSYAPALFNY MLELDQMRFK EISDDVKEKN
KNVLDFKWYT RKAESWGVQT FKNWKENLTI SEKDIITGYT GSKYDPINEY LRKYDGEIIP
NIGGDLDKKS KKALEKIENQ IKNLDAALQK SKITENLIVY RRVSELQFGK KYEDYNLRQN
GIINEEKVME LESNFKGQTF IQHNYMSTSL VQDPHQSYSN DRYPILLEIT IPEGVHGAYI
ADMSEYPGQY EMLINRGYTF KYDKFSIVKP TREEDKGKEY LKVNLSIYLG NLNREK
