ID   BINA3_LYSSH             Reviewed;         370 AA.
AC   P12963;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Binary larvicide subunit BinA {ECO:0000305};
DE   AltName: Full=41.9 kDa insecticidal toxin {ECO:0000303|PubMed:2798104};
DE   Flags: Precursor;
GN   Name=binA;
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   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). Binary toxin internalization into host
CC       gut cells requires both proteins (By similarity).
CC       {ECO:0000250|UniProtKB:P05516, ECO:0000269|PubMed:8419297}.
CC   -!- SUBUNIT: Forms a heterodimer with BinB. {ECO:0000250|UniProtKB:P06575}.
CC   -!- SUBCELLULAR LOCATION: Spore, perispore {ECO:0000250|UniProtKB:P05516}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates next to spores within the exosporeum.
CC       {ECO:0000250|UniProtKB:P05516}.
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 carbohydrate-binding modules while the barrel is involved in
CC       host cell receptor binding. At neutral pH the carbohydrate-binding
CC       modules are accessible on the toxin surface but the barrel subdomain is
CC       not. {ECO:0000250|UniProtKB:P06575}.
CC   -!- PTM: Processed by proteases in the mosquito gut, probably at both the
CC       N- and C-termini. {ECO:0000250|UniProtKB:P06575}.
CC   -!- SIMILARITY: Belongs to the toxin_10 family. {ECO:0000305}.
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DR   EMBL; X14964; CAA33087.1; -; Genomic_DNA.
DR   PIR; S07712; S07712.
DR   AlphaFoldDB; P12963; -.
DR   SMR; P12963; -.
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; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR008872; Toxin_P42.
DR   Pfam; PF05431; Toxin_10; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Sporulation; Toxin; Virulence.
FT   PROPEP          1..6
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT                   /id="PRO_0000448620"
FT   CHAIN           7..370
FT                   /note="Binary larvicide subunit BinA"
FT                   /id="PRO_0000174113"
FT   REGION          1..155
FT                   /note="Beta-trefoil domain"
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT   REGION          156..370
FT                   /note="Pore-forming domain"
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
SQ   SEQUENCE   370 AA;  41978 MW;  08B0D60DE4D1B0A8 CRC64;
     MRNLDFIDSF IPTEGKYIRV MDFYNSEYPF CIHAPSAPNG DIMTEICSRE NNQYFIFFPT
     DDGRVIIANR HNGSVFTGEA TSVVSDIYTG SPLQFFREVK RTMETYYLAI QNPESATDVR
     ALEPHSHELP SRLYYTNNIE NNSNILISNK EQIYLTLPSL PENEQYPKTP VLSGIDDIGP
     NQSEKSIIGS TLIPCIMVSD FISLGERMKT TPYYYVKHTQ YWQSMWSALF PPGSKETKTE
     KSGITDTSQI SMTDGINVSI GADFGLRFGN KTFGIKGGFT YDTKTQITNT SQLLIETTYT
     REYTNTENFP VRYTGYVLAS EFTLHRSDGT QVNTIPWVAL NDNYTTIARY PHFASEPLLG
     NTKIITDDQN