BINB1_LYSSH
ID BINB1_LYSSH Reviewed; 448 AA.
AC P10565;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Binary larvicide subunit BinB {ECO:0000305};
DE AltName: Full=63 kDa toxin crystal protein {ECO:0000303|PubMed:3926751};
DE AltName: Full=Binary paracrystalline larvicide subunit BinB {ECO:0000303|PubMed:27680699};
DE AltName: Full=Larvicidal toxin 51.4 kDa protein {ECO:0000303|PubMed:3360740};
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=ATCC 33203 / 1593;
RX PubMed=3412905; DOI=10.1093/nar/16.15.7731;
RA Arapinis C., de la Torre F., Szulmajster J.;
RT "Nucleotide and deduced amino acid sequence of the Bacillus sphaericus
RT 1593M gene encoding a 51.4 kD polypeptide which acts synergistically with
RT the 42 kD protein for expression of the larvicidal toxin.";
RL Nucleic Acids Res. 16:7731-7731(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2362;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33203 / 1593;
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 [4]
RP NO TOXIC FUNCTION ON ITS OWN, SUBUNIT, SUBCELLULAR LOCATION, AND
RP PROTEOLYTIC CLEAVAGE.
RC STRAIN=2362;
RX PubMed=3926751; DOI=10.1128/jb.163.2.738-747.1985;
RA Baumann P., Unterman B.M., Baumann L., Broadwell A.H., Abbene S.J.,
RA Bowditch R.D.;
RT "Purification of the larvicidal toxin of Bacillus sphaericus and evidence
RT for high-molecular-weight precursors.";
RL J. Bacteriol. 163:738-747(1985).
RN [5]
RP DEVELOPMENTAL STAGE.
RC STRAIN=2362;
RX PubMed=3777925; DOI=10.1128/aem.52.4.758-764.1986;
RA Broadwell A.H., Baumann P.;
RT "Sporulation-associated activation of Bacillus sphaericus larvicide.";
RL Appl. Environ. Microbiol. 52:758-764(1986).
RN [6]
RP TOXIN IS BINARY.
RC STRAIN=2362;
RX DOI=10.1007/BF02199438;
RA Broadwell A.H., Baumann L., Baumann P.;
RT "Larvicidal properties of the 42 and 51 kilodalton Bacillus sphaericus
RT proteins expressed in different bacterial hosts: evidence for a binary
RT toxin.";
RL Curr. Microbiol. 21:361-366(1990).
RN [7]
RP HOST RANGE.
RC STRAIN=2362;
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 [8]
RP INTERACTION WITH CULEX PIPIENS CPM1 RECEPTOR.
RC STRAIN=ATCC 33203 / 1593;
RX PubMed=11483434; DOI=10.1016/s0965-1748(01)00046-7;
RA Darboux I., Nielsen-LeRoux C., Charles J.F., Pauron D.;
RT "The receptor of Bacillus sphaericus binary toxin in Culex pipiens
RT (Diptera: Culicidae) midgut: molecular cloning and expression.";
RL Insect Biochem. Mol. Biol. 31:981-990(2001).
RN [9] {ECO:0007744|PDB:5FOY, ECO:0007744|PDB:5FOZ, ECO:0007744|PDB:5G37}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH BINA AT PH 5; PH 7
RP AND PH 10, SUBUNIT, DOMAIN, AND DISULFIDE BOND.
RC STRAIN=2362;
RX PubMed=27680699; DOI=10.1038/nature19825;
RA Colletier J.P., Sawaya M.R., Gingery M., Rodriguez J.A., Cascio D.,
RA Brewster A.S., Michels-Clark T., Hice R.H., Coquelle N., Boutet S.,
RA Williams G.J., Messerschmidt M., DePonte D.P., Sierra R.G., Laksmono H.,
RA Koglin J.E., Hunter M.S., Park H.W., Uervirojnangkoorn M., Bideshi D.K.,
RA Brunger A.T., Federici B.A., Sauter N.K., Eisenberg D.S.;
RT "De novo phasing with X-ray laser reveals mosquito larvicide BinAB
RT structure.";
RL Nature 539:43-47(2016).
CC -!- FUNCTION: Component of a binary toxin active against Culex and some
CC Aedes mosquito larvae (Ref.6, PubMed:8419297). This subunit alone has
CC no toxic larvicidal activity (PubMed:3926751). This subunit is
CC responsible for localized binding to specific regions of the host
CC larval gut. Binary toxin internalization into host gut cells requires
CC both proteins (By similarity). {ECO:0000250|UniProtKB:P18568,
CC ECO:0000269|PubMed:3926751, ECO:0000269|PubMed:8419297,
CC ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Forms a heterodimer with BinA (PubMed:27680699). Upon toxin
CC crystal solubilization with NaOH at pH 12, only the 63-kDa (binB) and
CC 43-kDa (binA) proteins were detected (PubMed:3926751). Interacts with
CC mosquito protein Cpm1 which acts as its host receptor
CC (PubMed:11483434). {ECO:0000269|PubMed:11483434,
CC ECO:0000269|PubMed:27680699, ECO:0000269|PubMed:3926751}.
CC -!- SUBCELLULAR LOCATION: Spore, perispore {ECO:0000305|PubMed:3926751}.
CC -!- DEVELOPMENTAL STAGE: Total crystal protein is produced during
CC sporulation, it appears after 6 hours of growth, and represents about
CC 4.8% of cellular dry weight in stationary phase. It probably
CC accumulates next to spores within the exosporeum.
CC {ECO:0000269|PubMed:3777925}.
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 (PubMed:27680699). The crystal is very stable at
CC neutral pH, upon ingestion by larvae the crystals dissolve in the
CC alkaline midgut. As the pH rises the 2 subunits compact, while
CC deprotonation at up to 4 sites (including the N- and C-termini)
CC increases the accessibility of the propeptides and moves subdomains.
CC The combined pH-induced changes are thought to expose the previously
CC hidden receptor-binding motif and lead to crystal dissolution
CC (Probable). {ECO:0000269|PubMed:27680699, ECO:0000305|PubMed:27680699}.
CC -!- PTM: Processed by proteases extracted from C.pipiens larval gut; unlike
CC its partner BinA, it does not form a stable digestion product.
CC {ECO:0000269|PubMed:3926751}.
CC -!- MISCELLANEOUS: In protein gels runs as a 63 kDa protein.
CC {ECO:0000269|PubMed:3412905, ECO:0000269|PubMed:3926751}.
CC -!- SIMILARITY: Belongs to the toxin_10 family. {ECO:0000305}.
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DR EMBL; X07992; CAA30800.1; -; Genomic_DNA.
DR EMBL; M20390; AAA22860.1; -; Genomic_DNA.
DR EMBL; AJ224477; CAB37654.1; -; Genomic_DNA.
DR PIR; A28211; A28211.
DR RefSeq; WP_012291792.1; NZ_LWHI01000001.1.
DR PDB; 5FOY; X-ray; 2.25 A; B=1-448.
DR PDB; 5FOZ; X-ray; 2.40 A; B=1-448.
DR PDB; 5G37; X-ray; 2.50 A; B=1-448.
DR PDBsum; 5FOY; -.
DR PDBsum; 5FOZ; -.
DR PDBsum; 5G37; -.
DR AlphaFoldDB; P10565; -.
DR SASBDB; P10565; -.
DR SMR; P10565; -.
DR TCDB; 1.C.4.7.1; the aerolysin channel-forming toxin (aerolysin) family.
DR OrthoDB; 1818676at2; -.
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 DisProt; DP03018; -.
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_0000174114"
FT REGION 1..198
FT /note="Beta-trefoil domain"
FT /evidence="ECO:0000269|PubMed:27680699"
FT REGION 199..448
FT /note="Probable pore-forming domain"
FT /evidence="ECO:0000269|PubMed:27680699"
FT DISULFID 67..161
FT /evidence="ECO:0000269|PubMed:27680699,
FT ECO:0007744|PDB:5FOY, ECO:0007744|PDB:5FOZ,
FT ECO:0007744|PDB:5G37"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5FOY"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5FOZ"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:5FOY"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5FOY"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5G37"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 259..277
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 358..372
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 378..396
FT /evidence="ECO:0007829|PDB:5FOY"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5FOY"
SQ SEQUENCE 448 AA; 51431 MW; 55112D0131BCE018 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 FGMLFYFRSS GFKEQITRGL NRPLSQTTTQ LGERVEEMEY YNSNDLDVRY
VKYALAREFT LKRVNGEIVK NWVAVDYRLA GIQSYPNAPI TNPLTLTKHT IIRCENSYDG
HIFKTPLIFK NGEVIVKTNE ELIPKINQ
