ID   CT2AA_BACTY             Reviewed;         259 AA.
AC   Q04470;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Type-2Aa cytolytic delta-endotoxin;
DE   AltName: Full=29 kDa cytolytic toxin;
GN   Name=cyt2Aa1; Synonyms=cytB;
OS   Bacillus thuringiensis subsp. kyushuensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=44161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8429550; DOI=10.1006/jmbi.1993.1037;
RA   Koni P.A., Ellar D.J.;
RT   "Cloning and characterization of a novel Bacillus thuringiensis cytolytic
RT   delta-endotoxin.";
RL   J. Mol. Biol. 229:319-327(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=8632451; DOI=10.1006/jmbi.1996.0152;
RA   Li J., Koni P.A., Ellar D.J.;
RT   "Structure of the mosquitocidal delta-endotoxin CytB from Bacillus
RT   thuringiensis sp. kyushuensis and implications for membrane pore
RT   formation.";
RL   J. Mol. Biol. 257:129-152(1996).
CC   -!- FUNCTION: Kills the larvae of dipteran insects by making pores in the
CC       epithelial cell membrane of the insect midgut.
CC   -!- SUBUNIT: Homodimer (protoxin) and monomer (active toxin).
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   -!- PTM: Active after proteolytic processing.
CC   -!- SIMILARITY: Belongs to the cyt1/cyt2 endotoxin family. {ECO:0000305}.
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DR   EMBL; Z14147; CAA78519.1; -; Genomic_DNA.
DR   PIR; S32432; S32432.
DR   RefSeq; WP_000288253.1; NZ_PGEE01000089.1.
DR   PDB; 1CBY; X-ray; 2.60 A; A=1-259.
DR   PDBsum; 1CBY; -.
DR   AlphaFoldDB; Q04470; -.
DR   SMR; Q04470; -.
DR   TCDB; 1.C.71.1.2; the cytolytic delta endotoxin (cyt1/2) family.
DR   EvolutionaryTrace; Q04470; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   Gene3D; 3.40.198.10; -; 1.
DR   InterPro; IPR035918; CytB_endotoxin-like_sf.
DR   InterPro; IPR001615; Endotoxin_CytB.
DR   Pfam; PF01338; Bac_thur_toxin; 1.
DR   SUPFAM; SSF55676; SSF55676; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Sporulation; Toxin; Virulence.
FT   CHAIN           1..259
FT                   /note="Type-2Aa cytolytic delta-endotoxin"
FT                   /id="PRO_0000174108"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           54..63
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           77..84
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   STRAND          90..106
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           107..122
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           129..141
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           146..149
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   STRAND          165..175
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   TURN            178..182
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   STRAND          183..197
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           199..202
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   STRAND          210..225
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   HELIX           233..237
FT                   /evidence="ECO:0007829|PDB:1CBY"
FT   STRAND          241..243
FT                   /evidence="ECO:0007829|PDB:1CBY"
SQ   SEQUENCE   259 AA;  29235 MW;  6924A01103D32B51 CRC64;
     MYTKNFSNSR MEVKGNNGCS APIIRKPFKH IVLTVPSSDL DNFNTVFYVQ PQYINQALHL
     ANAFQGAIDP LNLNFNFEKA LQIANGIPNS AIVKTLNQSV IQQTVEISVM VEQLKKIIQE
     VLGLVINSTS FWNSVEATIK GTFTNLDTQI DEAWIFWHSL SAHNTSYYYN ILFSIQNEDT
     GAVMAVLPLA FEVSVDVEKQ KVLFFTIKDS ARYEVKMKAL TLVQALHSSN APIVDIFNVN
     NYNLYHSNHK IIQNLNLSN