C35AB_BACTU
ID C35AB_BACTU Reviewed; 383 AA.
AC Q939S9;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Insecticidal crystal protein Cry35Ab1 {ECO:0000303|PubMed:11872461};
DE AltName: Full=44 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, POST-TRANSLATIONAL CLEAVAGE, 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, SUBUNIT, AND POST-TRANSLATIONAL CLEAVAGE.
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, AND BINDING TO HOST CELLS.
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:4JP0}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 355-LEU--PHE-383.
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 has no activity against southern corn rootworm (Diabrotica
CC undecimpunctata howardi Barber), but it synergizes the toxic effect of
CC its Cry34Ab1 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). Binds to WCR third
CC instar midgut brush border membrane vesicles; binding improves over 10-
CC fold in the presence of Cry34Ab1 (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 Cry34Ab1 (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 -!- PTM: Proteolytic processing occurs near the C-terminus yielding a
CC stable protein of approximately 40 kDa; this may be the active form of
CC the protein. {ECO:0000269|PubMed:11433280,
CC ECO:0000269|PubMed:15379574}.
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 -!- SIMILARITY: Belongs to the toxin_10 family. {ECO:0000305}.
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DR EMBL; AY011120; AAG41672.1; -; Genomic_DNA.
DR PDB; 4JP0; X-ray; 1.80 A; A=1-383.
DR PDBsum; 4JP0; -.
DR AlphaFoldDB; Q939S9; -.
DR SMR; Q939S9; -.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR008872; Toxin_P42.
DR Pfam; PF05431; Toxin_10; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Sporulation; Toxin; Virulence.
FT CHAIN 1..383
FT /note="Insecticidal crystal protein Cry35Ab1"
FT /id="PRO_0000448611"
FT DOMAIN 26..138
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT MUTAGEN 355..383
FT /note="Missing: No change in toxicity or in overall
FT structure, approximately equivalent to the truncated
FT protein isolated from parasporal inclusion bodies."
FT /evidence="ECO:0000269|PubMed:25390338"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4JP0"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4JP0"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 201..213
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:4JP0"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 307..336
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4JP0"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:4JP0"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:4JP0"
SQ SEQUENCE 383 AA; 43811 MW; DBA6C745268FF642 CRC64;
MLDTNKVYEI SNHANGLYAA TYLSLDDSGV SLMNKNDDDI DDYNLKWFLF PIDDDQYIIT
SYAANNCKVW NVNNDKINVS TYSSTNSIQK WQIKANGSSY VIQSDNGKVL TAGTGQALGL
IRLTDESSNN PNQQWNLTSV QTIQLPQKPI IDTKLKDYPK YSPTGNIDNG TSPQLMGWTL
VPCIMVNDPN IDKNTQIKTT PYYILKKYQY WQRAVGSNVA LRPHEKKSYT YEWGTEIDQK
TTIINTLGFQ INIDSGMKFD IPEVGGGTDE IKTQLNEELK IEYSHETKIM EKYQEQSEID
NPTDQSMNSI GFLTITSLEL YRYNGSEIRI MQIQTSDNDT YNVTSYPNHQ QALLLLTNHS
YEEVEEITNI PKSTLKKLKK YYF
