BINB2_LYSSH
ID BINB2_LYSSH Reviewed; 448 AA.
AC P18568; Q7B2I6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Binary larvicide subunit BinB {ECO:0000305};
DE AltName: Full=51.4 kDa insecticidal toxin;
DE AltName: Full=BinB protein {ECO:0000303|Ref.2};
DE AltName: Full=Larvicidal toxin protein P51 {ECO:0000303|PubMed:1512580};
GN Name=binB {ECO:0000303|Ref.2}; 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=2297;
RX PubMed=3360740; DOI=10.1128/jb.170.5.2045-2050.1988;
RA Baumann L., Broadwell A.H., Baumann P.;
RT "Sequence analysis of the mosquitocidal toxin genes encoding 51.4- and
RT 41.9-kilodalton proteins from Bacillus sphaericus 2362 and 2297.";
RL J. Bacteriol. 170:2045-2050(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2297;
RA Humphreys M.J., Coleman M.M., Berry C.;
RT "Transposition of Bacillus sphaericus toxin genes.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE, AND CRYSTAL DISSOLUTION FOLLOWING HOST FEEDING.
RC STRAIN=2297;
RX PubMed=16346157; DOI=10.1128/aem.44.6.1449-1455.1982;
RA Yousten A.A., Davidson E.W.;
RT "Ultrastructural analysis of spores and parasporal crystals formed by
RT Bacillus sphaericus 2297.";
RL Appl. Environ. Microbiol. 44:1449-1455(1982).
RN [4]
RP FUNCTION, HOST UPTAKE, AND MUTAGENESIS OF 1-MET--LYS-45; 1-MET--PRO-35;
RP 393-GLN--GLN-448 AND 397-ASN--GLN-448.
RC STRAIN=2297;
RX PubMed=1512580; DOI=10.1099/00221287-138-7-1515;
RA Oei C., Hindley J., Berry C.;
RT "Binding of purified Bacillus sphaericus binary toxin and its deletion
RT derivatives to Culex quinquefasciatus gut: elucidation of functional
RT binding domains.";
RL J. Gen. Microbiol. 138:1515-1526(1992).
RN [5]
RP FUNCTION, HOST RANGE, AND MUTAGENESIS OF 314-TYR--LEU-317.
RC STRAIN=2297;
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).
RN [6] {ECO:0007744|PDB:3WA1}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 19-407, DOMAIN, AND DISULFIDE
RP BONDS.
RC STRAIN=2297;
RX PubMed=24975613; DOI=10.1002/prot.24636;
RA Srisucharitpanit K., Yao M., Promdonkoy B., Chimnaronk S., Tanaka I.,
RA Boonserm P.;
RT "Crystal structure of BinB: a receptor binding component of the binary
RT toxin from Lysinibacillus sphaericus.";
RL Proteins 82:2703-2712(2014).
CC -!- FUNCTION: Component of a binary toxin active against Culex and some
CC Aedes mosquito larvae (PubMed:1512580, PubMed:8419297). This subunit is
CC responsible for localized binding to specific regions of the host
CC larval gut. The individual subunits are not toxic. BinAB and this
CC subunit alone bind to the gastric caecum and posterior midgut of
CC C.quinquefasciatus larvae. Binary toxin internalization into host gut
CC cells requires both proteins. Does not bind to the midgut of Aedes
CC aegypti (PubMed:1512580). Toxic to Aedes atropalpus mosquito larvae;
CC mortality towards both C.quinquefasciatus and A.atropalpus is maximal
CC by 48 hours. A.aegypti is not very susceptible to this toxin
CC (PubMed:8419297). Binding component of binary toxin. The 51 kDa
CC polypeptide acts synergetically with the 42 kDa polypeptide for
CC expression of a larvicidal toxin. {ECO:0000269|PubMed:1512580,
CC ECO:0000269|PubMed:8419297}.
CC -!- SUBUNIT: Forms a heterodimer with BinA. {ECO:0000250|UniProtKB:P10565}.
CC -!- SUBCELLULAR LOCATION: Spore, perispore {ECO:0000269|PubMed:16346157}.
CC -!- DEVELOPMENTAL STAGE: The parasporal crystal protein is produced during
CC sporulation and accumulates as a spore inclusion; crystals are
CC separated from the forespores by a branch of the exosporium across the
CC cell. The matrix of the paraspore is dissolved within 15 minutes
CC following C.quinquefasciatus larvae feeding.
CC {ECO:0000269|PubMed:16346157}.
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. {ECO:0000269|PubMed:24975613}.
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; AJ224478; CAB37657.1; -; Genomic_DNA.
DR PIR; C28211; C28211.
DR RefSeq; WP_036216621.1; NZ_JPDJ01000092.1.
DR PDB; 3WA1; X-ray; 1.75 A; A=19-407.
DR PDBsum; 3WA1; -.
DR AlphaFoldDB; P18568; -.
DR SMR; P18568; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Sporulation; Toxin; Virulence.
FT CHAIN 1..448
FT /note="Binary larvicide subunit BinB"
FT /id="PRO_0000174115"
FT REGION 19..200
FT /note="Beta-trefoil domain"
FT /evidence="ECO:0000269|PubMed:24975613"
FT REGION 226..407
FT /note="Probable pore-forming domain"
FT /evidence="ECO:0000269|PubMed:24975613"
FT DISULFID 67..161
FT /evidence="ECO:0000269|PubMed:24975613,
FT ECO:0007744|PDB:3WA1"
FT MUTAGEN 1..45
FT /note="Missing: In combination with whole BinA no longer
FT toxic, no longer binds to gastric caecum and posterior
FT midgut of larvae, BinA is no longer internalized."
FT /evidence="ECO:0000269|PubMed:1512580"
FT MUTAGEN 1..35
FT /note="Missing: In combination with whole BinA 5-fold
FT decrease in toxicity."
FT /evidence="ECO:0000269|PubMed:1512580"
FT MUTAGEN 314..317
FT /note="YFYL->LFYF: Increases toxicity against A.aegypti
FT larvae, protein is more like BinB from strain 2362."
FT /evidence="ECO:0000269|PubMed:8419297"
FT MUTAGEN 393..448
FT /note="Missing: In combination with whole BinA no longer
FT toxic, BinA is no longer internalized."
FT /evidence="ECO:0000269|PubMed:1512580"
FT MUTAGEN 397..448
FT /note="Missing: In combination with whole BinA 26-fold
FT decrease in toxicity."
FT /evidence="ECO:0000269|PubMed:1512580"
FT CONFLICT 338
FT /note="P -> T (in Ref. 2; CAB37657)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="H -> Y (in Ref. 2; CAB37657)"
FT /evidence="ECO:0000305"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3WA1"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3WA1"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3WA1"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 259..277
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:3WA1"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 358..372
FT /evidence="ECO:0007829|PDB:3WA1"
FT STRAND 378..396
FT /evidence="ECO:0007829|PDB:3WA1"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3WA1"
SQ SEQUENCE 448 AA; 51435 MW; 62C2F2B1BEDEB834 CRC64;
MCDSKDNSGV SEKCGKKFTN YPLNTTPTSL NYNLPEISKK FYNLKNKYSR NGYGLSKTEF
PSSIENCPSN EYSIMYDNKD PRFLIRFLLD DGRYIIADRD DGEVFDEAPT YLDNNNHPII
SRHYTGEERQ KFEQVGSGDY ITGEQFFQFY TQNKTRVLSN CRALDSRTIL LSTAKIFPIY
PPASETQLTA FVNSSFYAAA IPQLPQTSLL ENIPEPTSLD DSGVLPKDAV RAVKGSALLP
CIIVHDPNLN NSDKMKFNTY YLLEYKEYWH QLWSQIIPAH QTVKIQERTG ISEVVQNSMI
EDLNMYIGAD FGMYFYLRSS GFKEQITRGL NRPLSQTPTQ LGERVEEMEY YNSNDLDVRY
VKHALAREFT LKRVNGEIVK NWVAVDYRMA GIQSYPNAPI TNPLTLTKHT IIRCENSYDG
HIFKTPLIFK NGEVIVKTNE ELIPKINQ
