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 26-FEB-2020, entry version 64. 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; 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; 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:0000244|PDB:5FOY, ECO:0000244|PDB:5FOZ, ECO:0000244|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 wall, perispore CC {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P10565; -. DR TCDB; 1.C.4.7.1; the aerolysin channel-forming toxin (aerolysin) family. DR PRIDE; P10565; -. DR OrthoDB; 1818676at2; -. DR GO; GO:0031160; C:spore wall; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; 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_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:0000244|PDB:5FOY, ECO:0000244|PDB:5FOZ, FT ECO:0000244|PDB:5G37, ECO:0000269|PubMed:27680699" FT HELIX 36..38 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 39..48 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 54..56 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 71..73 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 75..81 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 84..88 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 94..98 FT /evidence="ECO:0000244|PDB:5FOY" FT TURN 99..101 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 104..107 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 113..115 FT /evidence="ECO:0000244|PDB:5FOZ" FT STRAND 117..122 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 128..130 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 131..138 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 140..142 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 146..151 FT /evidence="ECO:0000244|PDB:5FOY" FT TURN 152..155 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 156..162 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 164..166 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 168..174 FT /evidence="ECO:0000244|PDB:5FOY" FT TURN 179..182 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 185..189 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 191..198 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 218..220 FT /evidence="ECO:0000244|PDB:5G37" FT HELIX 226..228 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 232..240 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 241..243 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 251..257 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 259..277 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 282..290 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 293..303 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 304..308 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 313..315 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 317..320 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 323..330 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 343..351 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 354..356 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 358..372 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 378..396 FT /evidence="ECO:0000244|PDB:5FOY" FT TURN 398..400 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 404..413 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 425..429 FT /evidence="ECO:0000244|PDB:5FOY" FT HELIX 437..439 FT /evidence="ECO:0000244|PDB:5FOY" FT STRAND 442..444 FT /evidence="ECO:0000244|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 //