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BINA2_LYSSH
ID   BINA2_LYSSH             Reviewed;         370 AA.
AC   P05516;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Binary larvicide subunit BinA {ECO:0000305};
DE   AltName: Full=41.9 kDa insecticidal toxin {ECO:0000303|PubMed:3375083};
DE   AltName: Full=Larvicidal toxin protein P42 {ECO:0000303|PubMed:1512580};
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=2297;
RX   PubMed=3375083; DOI=10.1093/nar/16.9.4168;
RA   Hindley J., Berry C.;
RT   "Bacillus sphaericus strain 2297: nucleotide sequence of 41.9 kDa toxin
RT   gene.";
RL   Nucleic Acids Res. 16:4168-4168(1988).
RN   [2]
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   [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--ALA-34; 1-MET--TYR-17;
RP   350-TYR--ASN-370 AND 359-LEU--ASN-370.
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 PHE-99 AND SER-104.
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).
CC   -!- FUNCTION: Component of a binary toxin active against Culex and some
CC       Aedes mosquito larvae (PubMed:1512580, PubMed:8419297). The individual
CC       subunits are not toxic. BinAB binds to the gastric caecum and posterior
CC       midgut of C.quinquefasciatus larvae; this subunit alone binds the
CC       entire larval gut. Binary toxin internalization into host gut cells
CC       requires both proteins (PubMed:1512580). Toxic to Aedes atropalpus
CC       mosquito larvae; mortality towards both C.quinquefasciatus and
CC       A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible
CC       to this toxin (PubMed:8419297). {ECO:0000269|PubMed:1512580,
CC       ECO:0000269|PubMed:8419297}.
CC   -!- SUBUNIT: Forms a heterodimer with BinB. {ECO:0000250|UniProtKB:P06575}.
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 Culex 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 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. {ECO:0000250|UniProtKB:P06575}.
CC   -!- PTM: Processed by proteases in the mosquito gut, probably at both the
CC       N- and C-termini. {ECO:0000250|UniProtKB:P06575}.
CC   -!- SIMILARITY: Belongs to the toxin_10 family. {ECO:0000305}.
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DR   EMBL; X07025; CAA30074.1; -; Genomic_DNA.
DR   PIR; D28211; D28211.
DR   RefSeq; WP_036216620.1; NZ_JPDJ01000092.1.
DR   AlphaFoldDB; P05516; -.
DR   SMR; P05516; -.
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   Disulfide bond; Sporulation; Toxin; Virulence.
FT   PROPEP          1..6
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT                   /id="PRO_0000448619"
FT   CHAIN           7..370
FT                   /note="Binary larvicide subunit BinA"
FT                   /id="PRO_0000174112"
FT   REGION          1..155
FT                   /note="Beta-trefoil domain"
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT   REGION          156..370
FT                   /note="Pore-forming domain"
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000250|UniProtKB:P06575"
FT   MUTAGEN         1..34
FT                   /note="Missing: In combination with whole BinB no longer
FT                   toxic, binds larval gut, no longer internalized."
FT                   /evidence="ECO:0000269|PubMed:1512580"
FT   MUTAGEN         1..17
FT                   /note="Missing: In combination with whole BinB 15-fold
FT                   decrease in toxicity, binds larval gut, still
FT                   internalized."
FT                   /evidence="ECO:0000269|PubMed:1512580"
FT   MUTAGEN         99
FT                   /note="F->V: Increases early toxicity against
FT                   C.quinquefasciatus, enhances toxicity against A.aegypti
FT                   larvae, protein is more like BinA from strain 2362."
FT                   /evidence="ECO:0000269|PubMed:8419297"
FT   MUTAGEN         104
FT                   /note="S->A: No change in toxicity against
FT                   C.quinquefasciatus, slightly higher toxicity against
FT                   A.aegypti larvae, protein is more like BinA from strain
FT                   2362."
FT                   /evidence="ECO:0000269|PubMed:8419297"
FT   MUTAGEN         104
FT                   /note="S->E,G: 10- to 250-fold decrease in toxicity against
FT                   C.quinquefasciatus, not toxic against A.aegypti larvae,
FT                   protein is more like BinA from strain IAB59."
FT                   /evidence="ECO:0000269|PubMed:8419297"
FT   MUTAGEN         350..370
FT                   /note="Missing: In combination with whole BinB no longer
FT                   toxic, binds larval gut, no longer internalized."
FT                   /evidence="ECO:0000269|PubMed:1512580"
FT   MUTAGEN         359..370
FT                   /note="Missing: In combination with whole BinB 5-fold
FT                   decrease in toxicity, binds larval gut, still
FT                   internalized."
FT                   /evidence="ECO:0000269|PubMed:1512580"
SQ   SEQUENCE   370 AA;  41917 MW;  545D66F9505911D9 CRC64;
     MRNLDFIDSF IPTEGKYIRV MDFYNSEYPF CIHAPSAPNG DIMTEICSRE NNQYFIFFPT
     DDGRVIIANR HNGSVFTGEA TSVVSDIYTG SPLQFFREFK RTMSTYYLAI QNPESATDVR
     ALEPNSHELP SRLYFTNNIE NNSNILISNK EQIYLTLPSL PENEQYPKTP VLSGIDDIGP
     NQSEKSIIGS TLIPCIMVSD FISLGERMKT TPYYYVKHTQ YWQSMWSALF PPGSKETKTE
     KSGITDTSQI SMTDGINVSI GADFGLKFGN KTFGIKGGFT YDTKTQITNT SQLLIETTYT
     REYTNTENFP VRYTGYVLAS EFTLHRSDGT QVNTIPWVAL NDNYTTIARY PHFASEPLLG
     NTKIITDDQN
 
 
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