ID   BINB3_LYSSH             Reviewed;         448 AA.
AC   P12964;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Binary larvicide subunit BinB {ECO:0000305};
DE   AltName: Full=51.4 kDa insecticidal toxin {ECO:0000303|PubMed:2798104};
GN   Name=binB; Synonyms=sph04;
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAB59;
RX   PubMed=2798104; DOI=10.1093/nar/17.18.7516;
RA   Berry C., Jackson-Yap J., Oei C., Hindley J.;
RT   "Nucleotide sequence of two toxin genes from Bacillus sphaericus IAB59:
RT   sequence comparisons between five highly toxinogenic strains.";
RL   Nucleic Acids Res. 17:7516-7516(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=9002, IAB872, IAB881, and PR1;
RA   Humphreys M.J., Berry C.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   HOST RANGE.
RC   STRAIN=IAB59;
RX   PubMed=8419297; DOI=10.1128/jb.175.2.510-518.1993;
RA   Berry C., Hindley J., Ehrhardt A.F., Grounds T., de Souza I.,
RA   Davidson E.W.;
RT   "Genetic determinants of host ranges of Bacillus sphaericus mosquito
RT   larvicidal toxins.";
RL   J. Bacteriol. 175:510-518(1993).
CC   -!- FUNCTION: Component of a binary toxin active against Culex and some
CC       Aedes mosquito larvae; mortality towards both C.quinquefasciatus and
CC       A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible
CC       to this toxin (PubMed:8419297). This subunit is responsible for
CC       localized binding to specific regions of the host larval gut. Binary
CC       toxin internalization into host gut cells requires both proteins (By
CC       similarity). {ECO:0000250|UniProtKB:P18568,
CC       ECO:0000269|PubMed:8419297}.
CC   -!- SUBUNIT: Forms a heterodimer with BinA. {ECO:0000250|UniProtKB:P10565}.
CC   -!- SUBCELLULAR LOCATION: Spore, perispore {ECO:0000250|UniProtKB:P18568}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates next to spores within the exosporeum.
CC       {ECO:0000250|UniProtKB:P18568}.
CC   -!- DOMAIN: Has an N-terminal beta-trefoil domain and a C-terminal pore-
CC       forming domain. The trefoil domain has barrel and cap subdomains; the
CC       cap has 3 possible carbohydrate-binding modules while the barrel is
CC       involved in host cell receptor binding. At neutral pH the carbohydrate-
CC       binding modules are accessible on the toxin surface but the barrel
CC       subdomain is not. {ECO:0000250|UniProtKB:P10565}.
CC   -!- PTM: Processed by proteases extracted from mosquito larval gut.
CC       {ECO:0000250|UniProtKB:P10565}.
CC   -!- SIMILARITY: Belongs to the toxin_10 family. {ECO:0000305}.
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DR   EMBL; X14964; CAA33086.1; -; Genomic_DNA.
DR   EMBL; Y13311; CAA73752.1; -; Genomic_DNA.
DR   EMBL; Y13312; CAA73753.1; -; Genomic_DNA.
DR   EMBL; Y13313; CAA73754.1; -; Genomic_DNA.
DR   EMBL; Y13314; CAA73755.1; -; Genomic_DNA.
DR   PIR; S07711; S07711.
DR   AlphaFoldDB; P12964; -.
DR   SMR; P12964; -.
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   InterPro; IPR008872; Toxin_P42.
DR   Pfam; PF05431; Toxin_10; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Sporulation; Toxin; Virulence.
FT   CHAIN           1..448
FT                   /note="Binary larvicide subunit BinB"
FT                   /id="PRO_0000174116"
FT   REGION          1..198
FT                   /note="Beta-trefoil domain"
FT                   /evidence="ECO:0000250|UniProtKB:P10565"
FT   REGION          199..448
FT                   /note="Probable pore-forming domain"
FT                   /evidence="ECO:0000250|UniProtKB:P10565"
FT   DISULFID        67..161
FT                   /evidence="ECO:0000250|UniProtKB:P10565"
SQ   SEQUENCE   448 AA;  51431 MW;  D38422BF4607AA91 CRC64;
     MCDSKDNSGV SEKCGKKFTN YPLNTTPTSL NYNLPEISKK FYNLKNKYSR NGYGLSKTEF
     PSSIENCPAK EYSIMYDNKD PRFLIRFLLD DGRYIIADRD DGEVFDEAPI YLDNNNHPII
     SRHYTGEERQ KFEQVGSGDY ITGEQFFQFY TQNKTRVLSN CRALDSRTIL LSTAKIFPIY
     PPASETQLTA FVNSSFYAAA IPQLPQTSLL ENIPEPTSLD DSGVLPKDAV RAVKGSALLP
     CIIVHDPNLN NSDKMKFNTY YLLEYKEYWH QLWSQIIPAH QTVKIQERTG ISEVVQNSMI
     EDLNMYIGAD FGMHFYLRSS GFKEQITRGL NRPLSQTTTQ LGERVEEMEY YNSNDLDVRY
     VKYALAREFT LKRVNGEIVK NWVAVDYRLA GIQSYPNAPI TNPLTLTKHT IIRCENSYDG
     HIFKTPLIFK NGEVIVKTNE ELIPKINQ