C34AB_BACTU
ID C34AB_BACTU Reviewed; 123 AA.
AC Q939T0;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Insecticidal crystal protein Cry34Ab1 {ECO:0000303|PubMed:11872461};
DE AltName: Full=14 kDa insecticidal crystal protein {ECO:0000303|PubMed:11872461};
OS Bacillus thuringiensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE,
RP PROBABLE OPERON, AND BIOTECHNOLOGY.
RC STRAIN=PS149B1;
RX PubMed=11433280; DOI=10.1038/90282;
RA Moellenbeck D.J., Peters M.L., Bing J.W., Rouse J.R., Higgins L.S.,
RA Sims L., Nevshemal T., Marshall L., Ellis R.T., Bystrak P.G., Lang B.A.,
RA Stewart J.L., Kouba K., Sondag V., Gustafson V., Nour K., Xu D.,
RA Swenson J., Zhang J., Czapla T., Schwab G., Jayne S., Stockhoff B.A.,
RA Narva K., Schnepf H.E., Stelman S.J., Poutre C., Koziel M., Duck N.;
RT "Insecticidal proteins from Bacillus thuringiensis protect corn from corn
RT rootworms.";
RL Nat. Biotechnol. 19:668-672(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND PROBABLE OPERON.
RC STRAIN=PS149B1;
RX PubMed=11872461; DOI=10.1128/aem.68.3.1137-1145.2002;
RA Ellis R.T., Stockhoff B.A., Stamp L., Schnepf H.E., Schwab G.E., Knuth M.,
RA Russell J., Cardineau G.A., Narva K.E.;
RT "Novel Bacillus thuringiensis binary insecticidal crystal proteins active
RT on western corn rootworm, Diabrotica virgifera virgifera LeConte.";
RL Appl. Environ. Microbiol. 68:1137-1145(2002).
RN [3]
RP FUNCTION.
RC STRAIN=PS149B1;
RX PubMed=12076012; DOI=10.1603/0022-0493-95.3.635;
RA Herman R.A., Scherer P.N., Young D.L., Mihaliak C.A., Meade T.,
RA Woodsworth A.T., Stockhoff B.A., Narva K.E.;
RT "Binary insecticidal crystal protein from Bacillus thuringiensis, strain
RT PS149B1: effects of individual protein components and mixtures in
RT laboratory bioassays.";
RL J. Econ. Entomol. 95:635-639(2002).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=PS149B1;
RX PubMed=15379574; DOI=10.1021/bi048946z;
RA Masson L., Schwab G., Mazza A., Brousseau R., Potvin L., Schwartz J.L.;
RT "A novel Bacillus thuringiensis (PS149B1) containing a Cry34Ab1/Cry35Ab1
RT binary toxin specific for the western corn rootworm Diabrotica virgifera
RT virgifera LeConte forms ion channels in lipid membranes.";
RL Biochemistry 43:12349-12357(2004).
RN [5]
RP FUNCTION.
RC STRAIN=PS149B1;
RX PubMed=23308139; DOI=10.1371/journal.pone.0053079;
RA Li H., Olson M., Lin G., Hey T., Tan S.Y., Narva K.E.;
RT "Bacillus thuringiensis Cry34Ab1/Cry35Ab1 interactions with western corn
RT rootworm midgut membrane binding sites.";
RL PLoS ONE 8:E53079-E53079(2013).
RN [6] {ECO:0007744|PDB:4JOX}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT.
RX PubMed=25390338; DOI=10.1371/journal.pone.0112555;
RA Kelker M.S., Berry C., Evans S.L., Pai R., McCaskill D.G., Wang N.X.,
RA Russell J.C., Baker M.D., Yang C., Pflugrath J.W., Wade M., Wess T.J.,
RA Narva K.E.;
RT "Structural and biophysical characterization of Bacillus thuringiensis
RT insecticidal proteins Cry34Ab1 and Cry35Ab1.";
RL PLoS ONE 9:E112555-E112555(2014).
CC -!- FUNCTION: Component of a binary insecticidal toxin active on western
CC corn rootworm (WCR, Diabrotica virgifera subsp. virgifera Le Conte) and
CC probably also on northern corn rootworm (D.barberi). Both proteins are
CC required for maximal toxicity. The larval midgut epithelium is probably
CC the primary target (PubMed:11433280, PubMed:11872461). This protein
CC alone is also active against southern corn rootworm (Diabrotica
CC undecimpunctata howardi Barber), but its activity is synergized by its
CC Cry35Ab1 partner (PubMed:12076012). The 2 proteins individually and
CC together form ion channels; channels made in the presence of the 2
CC proteins have higher conductance (PubMed:15379574). Significantly
CC ameliorates the binding of Cry35Ab1 to WCR third instar midgut brush
CC border membrane vesicles. Binding of this protein by itself could not
CC be studied for technical reasons (PubMed:23308139).
CC {ECO:0000269|PubMed:11433280, ECO:0000269|PubMed:11872461,
CC ECO:0000269|PubMed:12076012, ECO:0000269|PubMed:15379574,
CC ECO:0000269|PubMed:23308139}.
CC -!- SUBUNIT: Monomer in solution (PubMed:25390338). Copurifies from
CC parasporal inclusion bodies with Cry35Ab1 (PubMed:11433280,
CC PubMed:11872461, PubMed:15379574). {ECO:0000269|PubMed:11433280,
CC ECO:0000269|PubMed:11872461, ECO:0000269|PubMed:15379574,
CC ECO:0000269|PubMed:25390338}.
CC -!- DEVELOPMENTAL STAGE: Expressed upon sporulation.
CC {ECO:0000269|PubMed:11433280}.
CC -!- INDUCTION: Probably part of the cry34Ab1-cry35Ab1 operon.
CC {ECO:0000305|PubMed:11433280, ECO:0000305|PubMed:11872461}.
CC -!- BIOTECHNOLOGY: Expression of the 2 toxin genes in transgenic corn
CC confers resistance to WCR and has been commercialized.
CC {ECO:0000269|PubMed:11433280}.
CC -!- MISCELLANEOUS: Iodination or fluorescein-5-maleimide modification makes
CC the protein non-toxic to WCR. {ECO:0000269|PubMed:23308139}.
CC -!- SIMILARITY: Belongs to the aegerolysin family. {ECO:0000305}.
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DR EMBL; AY011120; AAG41671.1; -; Genomic_DNA.
DR PDB; 4JOX; X-ray; 2.15 A; A=1-123.
DR PDBsum; 4JOX; -.
DR AlphaFoldDB; Q939T0; -.
DR SMR; Q939T0; -.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR009413; Aegerolysin-typ.
DR InterPro; IPR015926; Cytolysin/lectin.
DR Pfam; PF06355; Aegerolysin; 1.
DR SUPFAM; SSF63724; SSF63724; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Sporulation; Toxin; Virulence.
FT CHAIN 1..123
FT /note="Insecticidal crystal protein Cry34Ab1"
FT /id="PRO_0000448610"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:4JOX"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4JOX"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:4JOX"
SQ SEQUENCE 123 AA; 13602 MW; 79CA90BF1319515D CRC64;
MSAREVHIDV NNKTGHTLQL EDKTKLDGGR WRTSPTNVAN DQIKTFVAES NGFMTGTEGT
IYYSINGEAE ISLYFDNPFA GSNKYDGHSN KSQYEIITQG GSGNQSHVTY TIQTTSSRYG
HKS
