ID   CT2BA_BACTI             Reviewed;         263 AA.
AC   Q45723;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Type-2Ba cytolytic delta-endotoxin;
DE   AltName: Full=29 kDa cytolytic toxin;
GN   Name=cyt2Ba1; Synonyms=cyt2Ba7, cytB;
OS   Bacillus thuringiensis subsp. israelensis.
OG   Plasmid pRX80.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4Q2;
RX   PubMed=9212418; DOI=10.1128/aem.63.7.2716-2721.1997;
RA   Guerchicoff A., Ugalde R.A., Rubinstein C.P.;
RT   "Identification and characterization of a previously undescribed cyt gene
RT   in Bacillus thuringiensis subsp. israelensis.";
RL   Appl. Environ. Microbiol. 63:2716-2721(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T301;
RA   Yu J., Pang Y.;
RT   "Cloning and expression of a cyt2Ba gene from Bacillus thuringiensis,
RT   strain T301.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Kills the larvae of dipteran insects by making pores in the
CC       epithelial cell membrane of the insect midgut. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyt1/cyt2 endotoxin family. {ECO:0000305}.
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DR   EMBL; U52043; AAB63254.1; -; Genomic_DNA.
DR   EMBL; AF215645; AAF37222.1; -; Genomic_DNA.
DR   RefSeq; WP_000550493.1; NZ_VEIF01000053.1.
DR   RefSeq; YP_001573789.1; NC_010076.1.
DR   PDB; 2RCI; X-ray; 1.80 A; A=35-238.
DR   PDBsum; 2RCI; -.
DR   AlphaFoldDB; Q45723; -.
DR   SMR; Q45723; -.
DR   TCDB; 1.C.71.1.3; the cytolytic delta endotoxin (cyt1/2) family.
DR   EvolutionaryTrace; Q45723; -.
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; Plasmid; Sporulation; Toxin; Virulence.
FT   CHAIN           1..263
FT                   /note="Type-2Ba cytolytic delta-endotoxin"
FT                   /id="PRO_0000174109"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           78..87
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   STRAND          91..107
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           108..123
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           130..144
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   STRAND          156..161
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   STRAND          166..176
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   STRAND          184..198
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:2RCI"
FT   STRAND          211..226
FT                   /evidence="ECO:0007829|PDB:2RCI"
SQ   SEQUENCE   263 AA;  29843 MW;  47545F67B49EBABD CRC64;
     MHLNNLNNFN NLENNGEYHC SGPIIKKPFR HIALTVPSSD ITNFNEIFYV EPQYIAQAIR
     LTNTFQGAID PLTLNFNFEK ALQIANGLPN AGVTGTINQS VIHQTIEVSV MISQIKEIIR
     SVLGLVINSA NFWNSVVSAI TNTFTNLEPQ VDENWIVWRN LSATQTSYFY KILFSIQNED
     TGRFMAILPI AFEITVDVQK QQLLFITIKD SARYEVKMKA LTVVQALDSY NAPIIDVFNV
     RNYSLHRPNH NILQNLNVNP IKS