CR3AA_BACTT
ID CR3AA_BACTT Reviewed; 644 AA.
AC P0A379; P07130; P21255;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Pesticidal crystal protein Cry3Aa;
DE AltName: Full=73 kDa crystal protein;
DE AltName: Full=Crystaline entomocidal protoxin;
DE AltName: Full=Insecticidal delta-endotoxin CryIIIA(a);
DE Flags: Precursor;
GN Name=cry3Aa; Synonyms=bt13, cry3A, cryC, cryIIIa, cryIIIA(a);
OS Bacillus thuringiensis subsp. tenebrionis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1444;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3658680; DOI=10.1093/nar/15.17.7183;
RA Hoefte H., Seurinck J., Houtven A.V., Vaeck M.;
RT "Nucleotide sequence of a gene encoding an insecticidal protein of Bacillus
RT thuringiensis var. tenebrionis toxic against Coleoptera.";
RL Nucleic Acids Res. 15:7183-7183(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593878; DOI=10.1073/pnas.84.20.7036;
RA Sekar V., Thompson D.V., Maroney M.J., Bookland R.G., Adang M.J.;
RT "Molecular cloning and characterization of the insecticidal crystal protein
RT gene of Bacillus thuringiensis var. tenebrionis.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7036-7040(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA McPherson S.A., Perlak F.J., Fuchs R.L., Marrone P.G., Lavrik P.B.,
RA Fischhoff D.A.;
RT "Characterization of the coleopteran-specific protein gene of Bacillus
RT thuringiensis var. tenebrionis.";
RL Biotechnology (N.Y.) 6:61-66(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NB176;
RX PubMed=7830581; DOI=10.1111/j.1365-2958.1994.tb01298.x;
RA Adams L.F., Mathewes S., O'Hara P., Petersen A., Gurtler H.;
RT "Elucidation of the mechanism of CryIIIA overproduction in a mutagenized
RT strain of Bacillus thuringiensis var. tenebrionis.";
RL Mol. Microbiol. 14:381-389(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1658659; DOI=10.1038/353815a0;
RA Li J., Carroll J., Ellar D.J.;
RT "Crystal structure of insecticidal delta-endotoxin from Bacillus
RT thuringiensis at 2.5-A resolution.";
RL Nature 353:815-821(1991).
CC -!- FUNCTION: Promotes colloidosmotic lysis by binding to the midgut
CC epithelial cells of Coleoptera.
CC -!- DEVELOPMENTAL STAGE: The crystal protein is produced during sporulation
CC and is accumulated both as an inclusion and as part of the spore coat.
CC -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC insect-resistant potato by Monsanto.
CC -!- MISCELLANEOUS: Toxic segment of the protein is located in the N-
CC terminus.
CC -!- SIMILARITY: Belongs to the delta endotoxin family. {ECO:0000305}.
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DR EMBL; Y00420; CAA68482.1; -; Genomic_DNA.
DR EMBL; J02978; AAA22541.1; -; Genomic_DNA.
DR EMBL; M30503; AAA22542.1; -; Genomic_DNA.
DR EMBL; U10985; AAC43266.1; -; Genomic_DNA.
DR PDB; 1DLC; X-ray; 2.50 A; A=61-644.
DR PDB; 4QX0; X-ray; 2.80 A; A=58-644.
DR PDB; 4QX1; X-ray; 2.80 A; A=58-644.
DR PDB; 4QX2; X-ray; 2.90 A; A=58-644.
DR PDB; 4QX3; X-ray; 2.90 A; A=58-644.
DR PDBsum; 1DLC; -.
DR PDBsum; 4QX0; -.
DR PDBsum; 4QX1; -.
DR PDBsum; 4QX2; -.
DR PDBsum; 4QX3; -.
DR AlphaFoldDB; P0A379; -.
DR SMR; P0A379; -.
DR PRIDE; P0A379; -.
DR EvolutionaryTrace; P0A379; -.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0001897; P:cytolysis by symbiont of host cells; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.20.190.10; -; 1.
DR Gene3D; 2.100.10.10; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038979; Pest_crys.
DR InterPro; IPR005638; Pest_crys_C.
DR InterPro; IPR005639; Pest_crys_N.
DR InterPro; IPR036716; Pest_crys_N_sf.
DR InterPro; IPR001178; Pest_cryst_cen_dom.
DR InterPro; IPR036399; Pest_cryst_cen_dom_sf.
DR PANTHER; PTHR37003; PTHR37003; 1.
DR Pfam; PF03944; Endotoxin_C; 1.
DR Pfam; PF00555; Endotoxin_M; 1.
DR Pfam; PF03945; Endotoxin_N; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51096; SSF51096; 1.
DR SUPFAM; SSF56849; SSF56849; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Genetically modified food; Sporulation; Toxin; Virulence.
FT PROPEP 1..57
FT /note="Removed in mature form"
FT /id="PRO_0000006345"
FT CHAIN 58..644
FT /note="Pesticidal crystal protein Cry3Aa"
FT /id="PRO_0000006346"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 544
FT /note="G -> A (in Ref. 3; AAA22542)"
FT /evidence="ECO:0000305"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 123..152
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 160..180
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1DLC"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 194..214
FT /evidence="ECO:0007829|PDB:1DLC"
FT TURN 215..219
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 222..253
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1DLC"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 335..347
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 356..369
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 398..411
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 414..428
FT /evidence="ECO:0007829|PDB:1DLC"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 471..480
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 542..550
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 560..571
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 582..589
FT /evidence="ECO:0007829|PDB:1DLC"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 618..625
FT /evidence="ECO:0007829|PDB:1DLC"
FT STRAND 633..643
FT /evidence="ECO:0007829|PDB:1DLC"
SQ SEQUENCE 644 AA; 73109 MW; EFCFF1CEEFDA9683 CRC64;
MNPNNRSEHD TIKTTENNEV PTNHVQYPLA ETPNPTLEDL NYKEFLRMTA DNNTEALDSS
TTKDVIQKGI SVVGDLLGVV GFPFGGALVS FYTNFLNTIW PSEDPWKAFM EQVEALMDQK
IADYAKNKAL AELQGLQNNV EDYVSALSSW QKNPVSSRNP HSQGRIRELF SQAESHFRNS
MPSFAISGYE VLFLTTYAQA ANTHLFLLKD AQIYGEEWGY EKEDIAEFYK RQLKLTQEYT
DHCVKWYNVG LDKLRGSSYE SWVNFNRYRR EMTLTVLDLI ALFPLYDVRL YPKEVKTELT
RDVLTDPIVG VNNLRGYGTT FSNIENYIRK PHLFDYLHRI QFHTRFQPGY YGNDSFNYWS
GNYVSTRPSI GSNDIITSPF YGNKSSEPVQ NLEFNGEKVY RAVANTNLAV WPSAVYSGVT
KVEFSQYNDQ TDEASTQTYD SKRNVGAVSW DSIDQLPPET TDEPLEKGYS HQLNYVMCFL
MQGSRGTIPV LTWTHKSVDF FNMIDSKKIT QLPLVKAYKL QSGASVVAGP RFTGGDIIQC
TENGSAATIY VTPDVSYSQK YRARIHYAST SQITFTLSLD GAPFNQYYFD KTINKGDTLT
YNSFNLASFS TPFELSGNNL QIGVTGLSAG DKVYIDKIEF IPVN
