CR1BE_BACTU
ID CR1BE_BACTU Reviewed; 1227 AA.
AC O85805;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Pesticidal crystal protein Cry1Be;
DE AltName: Full=139 kDa crystal protein;
DE AltName: Full=Crystaline entomocidal protoxin;
DE AltName: Full=Insecticidal delta-endotoxin CryIB(e);
GN Name=cry1Be; Synonyms=158C2B, cryIB(e);
OS Bacillus thuringiensis.
OG Plasmid pMYC2383.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRRL B-18872 / PS158C2;
RA Payne J.M., Cummings D.A., Cannon R.J.C., Narva K.E., Stelman S.;
RT "Bacillus thuringiensis genes encoding lepidopteran-active toxins.";
RL Patent number US5723758, 03-MAR-1998.
CC -!- FUNCTION: Promotes colloidosmotic lysis by binding to the midgut
CC epithelial cells of many lepidopteran larvae.
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 -!- MISCELLANEOUS: Toxic segment of the protein is located in the N-
CC terminus.
CC -!- SIMILARITY: Belongs to the delta endotoxin 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; AF077326; AAC32850.1; -; Genomic_DNA.
DR PDB; 6OWK; X-ray; 2.70 A; A=35-510.
DR PDBsum; 6OWK; -.
DR AlphaFoldDB; O85805; -.
DR SMR; O85805; -.
DR PRIDE; O85805; -.
DR ABCD; O85805; 3 sequenced antibodies.
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; -; 1.
DR InterPro; IPR041587; Cry_V.
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; IPR001178; Pest_cryst_cen_dom.
DR InterPro; IPR036399; Pest_cryst_cen_dom_sf.
DR PANTHER; PTHR37003; PTHR37003; 1.
DR Pfam; PF17997; Cry1Ac_D5; 1.
DR Pfam; PF03944; Endotoxin_C; 1.
DR Pfam; PF00555; Endotoxin_M; 1.
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 3D-structure; Plasmid; Sporulation; Toxin; Virulence.
FT CHAIN 1..1227
FT /note="Pesticidal crystal protein Cry1Be"
FT /id="PRO_0000174034"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 114..141
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 150..171
FT /evidence="ECO:0007829|PDB:6OWK"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 182..206
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 210..241
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 247..263
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:6OWK"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6OWK"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 347..364
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 393..405
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 410..422
FT /evidence="ECO:0007829|PDB:6OWK"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 438..447
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 480..489
FT /evidence="ECO:0007829|PDB:6OWK"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:6OWK"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:6OWK"
SQ SEQUENCE 1227 AA; 139085 MW; CBA847BEA0B34CD3 CRC64;
MTSNRKNENE IINALSIPAV SNHSAQMNLS TDARIEDSLC IAEGNNIDPF VSASTVQTGI
NIAGRILGVL GVPFAGQIAS FYSFLVGELW PRGRDPWEIF LEHVEQLIRQ QVTENTRDTA
LARLQGLGNS FRAYQQSLED WLENRDDART RSVLYTQYIA LELDFLNAMP LFAIRNQEVP
LLMVYAQAAN LHLLLLRDAS LFGSEFGLTS QEIQRYYERQ VEKTREYSDY CARWYNTGLN
NLRGTNAESW LRYNQFRRDL TLGVLDLVAL FPSYDTRVYP MNTSAQLTRE IYTDPIGRTN
APSGFASTNW FNNNAPSFSA IEAAVIRPPH LLDFPEQLTI FSVLSRWSNT QYMNYWVGHR
LESRTIRGSL STSTHGNTNT SINPVTLQFT SRDVYRTESF AGINILLTTP VNGVPWARFN
WRNPLNSLRG SLLYTIGYTG VGTQLFDSET ELPPETTERP NYESYSHRLS NIRLISGNTL
RAPVYSWTHR SADRTNTISS DSITQIPLVK SFNLNSGTSV VSGPGFTGGD IIRTNVNGSV
LSMGLNFNNT SLQRYRVRVR YAASQTMVLR VTVGGSTTFD QGFPSTMSAN ESLTSQSFRF
AEFPVGISAS GSQTAGISIS NNAGRQTFHF DKIEFIPITA TFEAEYDLER AQEAVNALFT
NTNPRRLKTG VTDYHIDEVS NLVACLSDEF CLDEKRELLE KVKYAKRLSD ERNLLQDPNF
TSINKQPDFI STNEQSNFTS IHEQSEHGWW GSENITIQEG NDVFKENYVI LPGTFNECYP
TYLYQKIGEA ELKAYTRYQL SGYIEDSQDL EIYLIRYNAK HETLDVPGTE SVWPLSVESP
IGRCGEPNRC APHFEWNPDL DCSCRDGEKC AHHSHHFSLD IDVGCIDLHE NLGVWVVFKI
KTQEGHARLG NLEFIEEKPL LGEALSRVKR AEKKWRDKRE KLQLETKRVY TEAKEAVDAL
FVDSQYDRLQ ADTNIGMIHA ADKLVHRIRE AYLSELSVIP GVNAEIFEEL EGRIITAISL
YDARNVVKNG DFNNGLACWN VKGHVDVQQS HHRSVLVIPE WEAEVSQAVR VCPGRGYILR
VTAYKEGYGE GCVTIHEIEN NTDELKFKNC EEEEVYPTDT GTCNDYTAHQ GTAACNSRNA
GYEDAYEVDT TASVNYKPTY EEETYTDVRR DNHCEYDRGY VNYPPVPAGY MTKELEYFPE
TDKVWIEIGE TEGKFIVDSV ELLLMEE