BINA1_LYSSH
ID BINA1_LYSSH Reviewed; 370 AA.
AC P06575;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Binary larvicide subunit BinA {ECO:0000305};
DE AltName: Full=41.9 kDa insecticidal toxin {ECO:0000303|PubMed:3615208};
DE AltName: Full=Binary paracrystalline larvicide subunit BinA {ECO:0000303|PubMed:27680699};
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=2362;
RX PubMed=3615208; DOI=10.1093/nar/15.14.5891;
RA Berry C., Hindley J.;
RT "Bacillus sphaericus strain 2362: identification and nucleotide sequence of
RT the 41.9 kDa toxin gene.";
RL Nucleic Acids Res. 15:5891-5891(1987).
RN [2]
RP ERRATUM OF PUBMED:3615208.
RA Berry C., Hindley J.;
RT "Bacillus sphaericus strain 2362: identification and nucleotide sequence of
RT the 41.9 kDa toxin gene.";
RL Nucleic Acids Res. 15:7216-7216(1987).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33203 / 1593;
RX PubMed=3449740; DOI=10.1111/j.1365-2958.1987.tb00511.x;
RA Hindley J., Berry C.;
RT "Identification, cloning and sequence analysis of the Bacillus sphaericus
RT 1593 41.9 kD larvicidal toxin gene.";
RL Mol. Microbiol. 1:187-194(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2317.3;
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 5-44, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, PROTEOLYTIC CLEAVAGE, AND HOST RANGE.
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 [8]
RP PROTEIN SEQUENCE OF 7-14, FUNCTION, ACTIVITY REGULATION, AND PROTEOLYTIC
RP CLEAVAGE.
RC STRAIN=2362;
RX PubMed=2886104; DOI=10.1128/aem.53.6.1333-1337.1987;
RA Broadwell A.H., Baumann P.;
RT "Proteolysis in the gut of mosquito larvae results in further activation of
RT the Bacillus sphaericus toxin.";
RL Appl. Environ. Microbiol. 53:1333-1337(1987).
RN [9]
RP FUNCTION, AND 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 [10]
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 [11]
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 [12] {ECO:0007744|PDB:5FOY, ECO:0007744|PDB:5FOZ, ECO:0007744|PDB:5G37}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH BINB AT PH 5; PH 7
RP AND PH 10, SUBUNIT, DOMAIN, MUTAGENESIS OF ASP-22, 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; about 1000-fold more toxic against
CC C.quinquefasciatus than A.aegypti (Probable) (Ref.10, PubMed:8419297).
CC This subunit alone is active against C.quinquefasciatus, Anopheles
CC gambiae, A.stephensi and Aedes aegypti mosquito cell lines; non Culex
CC mosquitoes are less sensitive to the toxin (PubMed:2886104) (Probable).
CC Binary toxin internalization into host gut cells requires both proteins
CC (By similarity). {ECO:0000250|UniProtKB:P05516,
CC ECO:0000269|PubMed:2886104, ECO:0000269|PubMed:8419297,
CC ECO:0000269|Ref.10, ECO:0000305|PubMed:3777925,
CC ECO:0000305|PubMed:3926751}.
CC -!- ACTIVITY REGULATION: Toxic activity of the cleaved 40 kDa form of this
CC subunit alone on cells of C.quinquefasciatus is decreased about 50% by
CC chitobiose, chitotriose, N-acetylmuramic acid and N-acetylneuraminic
CC acid. {ECO:0000269|PubMed:2886104}.
CC -!- SUBUNIT: Forms a heterodimer with BinB (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).
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, appears after 6 hours of growth, and represents about 4.8%
CC of cellular dry weight in stationary phase. It probably accumulates
CC next to spores within the exosporeum. {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 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 (PubMed:27680699). The crystal is very stable at neutral pH, upon
CC ingestion by larvae the crystals dissolve in the alkaline midgut. As
CC the pH rises the 2 subunits compact, while deprotonation at up to 4
CC sites (including the N- and C-termini) increases the accessibility of
CC the propeptides and moves subdomains. The combined pH-induced changes
CC are thought to expose the previously hidden receptor-binding motif and
CC lead to crystal dissolution (Probable). {ECO:0000269|PubMed:27680699,
CC ECO:0000305|PubMed:27680699}.
CC -!- PTM: Processed by proteases extracted from C.pipiens larval gut; 6
CC amino acids are removed from the N-terminus while it is estimated about
CC 20 residues are removed from the C-terminus to yield the 40 kDa toxin
CC form that is seen in insects. The 40 kDa form is 50-fold more lethal
CC against tissue culture cells than the precursor form. Larval gut
CC extracts of Aedes aegypti and Anopheles gambiae also generate the same
CC 40 kDa form all of which are toxic in C.pipiens.
CC {ECO:0000269|PubMed:2886104, ECO:0000305|PubMed:3926751}.
CC -!- SIMILARITY: Belongs to the toxin_10 family. {ECO:0000305}.
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DR EMBL; Y00378; CAA68450.1; -; Genomic_DNA.
DR EMBL; M20390; AAA22861.1; -; Genomic_DNA.
DR EMBL; M36957; AAA22862.1; -; mRNA.
DR EMBL; AJ224477; CAB37655.1; -; Genomic_DNA.
DR PIR; A27098; A27098.
DR RefSeq; WP_012291791.1; NZ_LWHI01000001.1.
DR PDB; 5FOY; X-ray; 2.25 A; A=1-370.
DR PDB; 5FOZ; X-ray; 2.40 A; A=1-370.
DR PDB; 5G37; X-ray; 2.50 A; A=1-366.
DR PDBsum; 5FOY; -.
DR PDBsum; 5FOZ; -.
DR PDBsum; 5G37; -.
DR AlphaFoldDB; P06575; -.
DR SMR; P06575; -.
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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR008872; Toxin_P42.
DR Pfam; PF05431; Toxin_10; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Sporulation;
KW Toxin; Virulence.
FT PROPEP 1..6
FT /evidence="ECO:0000269|PubMed:2886104"
FT /id="PRO_0000448618"
FT CHAIN 7..370
FT /note="Binary larvicide subunit BinA"
FT /id="PRO_0000174111"
FT REGION 1..155
FT /note="Beta-trefoil domain"
FT /evidence="ECO:0000269|PubMed:27680699"
FT REGION 156..370
FT /note="Pore-forming domain"
FT /evidence="ECO:0000269|PubMed:27680699"
FT DISULFID 31..47
FT /evidence="ECO:0000269|PubMed:27680699,
FT ECO:0007744|PDB:5FOY, ECO:0007744|PDB:5FOZ,
FT ECO:0007744|PDB:5G37"
FT MUTAGEN 22
FT /note="D->N: Decreased heterodimer solubility at pH 10, 10-
FT 20 fold less toxic to C.quinquefasciatus 4th instar
FT larvae."
FT /evidence="ECO:0000269|PubMed:27680699"
FT CONFLICT 31
FT /note="C -> S (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000269|PubMed:3926751"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5FOY"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 212..230
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5FOY"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5FOY"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 311..325
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 337..351
FT /evidence="ECO:0007829|PDB:5FOY"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:5FOY"
SQ SEQUENCE 370 AA; 41920 MW; BCB0D759A0D1B2D1 CRC64;
MRNLDFIDSF IPTEGKYIRV MDFYNSEYPF CIHAPSAPNG DIMTEICSRE NNQYFIFFPT
DDGRVIIANR HNGSVFTGEA TSVVSDIYTG SPLQFFREVK RTMATYYLAI 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
