ID   C18AA_PAEPP             Reviewed;         706 AA.
AC   Q45358;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Parasporal crystal protein Cry18Aa;
DE   AltName: Full=79 kDa crystal protein;
DE   AltName: Full=Crystaline parasporal protoxin;
DE   AltName: Full=Parasporal delta-endotoxin CryXVIIIA(a);
GN   Name=cry18Aa; Synonyms=cryBP1, cryXVIIIA(a);
OS   Paenibacillus popilliae (Bacillus popilliae).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=78057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=H1 / subsp. melolonthae;
RX   PubMed=9209052; DOI=10.1128/jb.179.13.4336-4341.1997;
RA   Zhang J., Hodgman T.C., Krieger L., Schnetter W., Schairer H.U.;
RT   "Cloning and analysis of the first cry gene from Bacillus popilliae.";
RL   J. Bacteriol. 179:4336-4341(1997).
CC   -!- FUNCTION: Binds to the brush border membrane vesicles of scarab larvae
CC       and somehow damages the gut wall to allow the vegetative cells of
CC       P.popilliae to enter the hemolymph. Active on M.melolontha.
CC   -!- DEVELOPMENTAL STAGE: The crystal protein is produced during sporulation
CC       and is accumulated both as an inclusion and as part of the spore coat.
CC   -!- SIMILARITY: Belongs to the delta endotoxin family. {ECO:0000305}.
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DR   EMBL; X99049; CAA67506.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q45358; -.
DR   SMR; Q45358; -.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0001897; P:cytolysis by symbiont of host cells; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.190.10; -; 1.
DR   Gene3D; 2.100.10.10; -; 2.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR038979; Pest_crys.
DR   InterPro; IPR005638; Pest_crys_C.
DR   InterPro; IPR005639; Pest_crys_N.
DR   InterPro; IPR036716; Pest_crys_N_sf.
DR   InterPro; IPR015214; Pest_cryst_cen_dom_Cry2A/18.
DR   InterPro; IPR036399; Pest_cryst_cen_dom_sf.
DR   PANTHER; PTHR37003; PTHR37003; 1.
DR   Pfam; PF03944; Endotoxin_C; 1.
DR   Pfam; PF09131; Endotoxin_mid; 2.
DR   Pfam; PF03945; Endotoxin_N; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51096; SSF51096; 1.
DR   SUPFAM; SSF56849; SSF56849; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Sporulation; Toxin; Virulence.
FT   CHAIN           1..706
FT                   /note="Parasporal crystal protein Cry18Aa"
FT                   /id="PRO_0000174091"
FT   CONFLICT        670
FT                   /note="T -> F (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   706 AA;  79035 MW;  9172B949BE499C1D CRC64;
     MNNNFNGGNN TGNNFTGNTL SNGICTKKNM KGTLSRTAIF SDGISDDLIC CLDPIYNNND
     NNNDAICDEL GLTPIDNNTI CSTDFTPINV MRTDPFRKKS TQELTREWTE WKENSPSLFT
     PAIVGVVTSF LLQSLKKQAT SFLLKTLTDL LFPNNSSLTM EEILRATEQY VQERLDTDTA
     NRVSQELVGL KNNLTTFNDQ VEDFLQNRVG ISPLAIIDSI NTMQQLFVNR LPQFQVSGYQ
     VLLLPLFAQA ATLHLTFLRD VIINADEWNI PTAQLNTYTR YFKEYIAEYS NYALSTYDDG
     FRTRFYPRNT LEDMLQFKTF MTLNALDLVS IWSLLKYVNL YVSTSANLYN IGDNKVNEGA
     YPISYGPFFN SYIQTKSNYV LSGVSGIGAR FTYSTVLGRY LHDDLKNIIT TYVGGTQGPN
     IGVQLSTTEL DELKKQQQAT RDSLVDFQFF TLNCMLPNPI TAPYFATSLY ESRYSSIGGY
     LRKDVFKSED STCGLGNPGA WTSYPDYYIT NISATVQING ENTDTTPLYF KENRPITSTR
     GVNKVIAVYN RKANIAGTNQ NGTMIHQAPP DGTGFTVSPL HPSANTITSY IKENYGNSGD
     SLHLKGQGYL HYMLSGNGQD RYRLVLRLSG AANQIKLQSP TTSIYAFDTS TNNEGITDNG
     SKFKDFAFST PFVIPEQKEI VLYFEGVGSL DLMNLIFLPA DDTPLY