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 07-OCT-2020, entry version 50. 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; 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:0000244|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 wall, perispore CC {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}. 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; 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 SMR; P18568; -. 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_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:0000244|PDB:3WA1, FT ECO:0000269|PubMed:24975613" 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:0000244|PDB:3WA1" FT STRAND 39..48 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 54..56 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 75..81 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 84..88 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 94..98 FT /evidence="ECO:0000244|PDB:3WA1" FT TURN 99..101 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 104..107 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 113..115 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 117..122 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 128..130 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 132..138 FT /evidence="ECO:0000244|PDB:3WA1" FT TURN 140..142 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 145..151 FT /evidence="ECO:0000244|PDB:3WA1" FT TURN 152..155 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 156..162 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 164..166 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 168..174 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 179..181 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 184..189 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 191..198 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 226..228 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 232..240 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 241..243 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 251..257 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 259..277 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 282..290 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 293..303 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 304..308 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 313..315 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 317..320 FT /evidence="ECO:0000244|PDB:3WA1" FT HELIX 323..330 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 338..340 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 343..351 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 354..356 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 358..372 FT /evidence="ECO:0000244|PDB:3WA1" FT STRAND 378..396 FT /evidence="ECO:0000244|PDB:3WA1" FT TURN 398..400 FT /evidence="ECO:0000244|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 //