CR2AA_BACTK
ID CR2AA_BACTK Reviewed; 633 AA.
AC P0A377; O52764; P21253;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Pesticidal crystal protein Cry2Aa;
DE AltName: Full=71 kDa crystal protein;
DE AltName: Full=Crystaline entomocidal protoxin;
DE AltName: Full=Insecticidal delta-endotoxin CryIIA(a);
DE AltName: Full=Mosquito factor;
DE AltName: Full=P2 crystal protein {ECO:0000303|PubMed:3121615};
GN Name=cry2Aa; Synonyms=cryB1 {ECO:0000303|PubMed:2914879}, cryII, cryIIA(a);
OS Bacillus thuringiensis subsp. kurstaki.
OG Plasmid unnamed.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29339;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INSECT TOXICITY, INDUCTION, AND OPERON.
RC STRAIN=HD-1;
RX PubMed=2914879; DOI=10.1128/jb.171.2.965-974.1989;
RA Widner W.R., Whiteley H.R.;
RT "Two highly related insecticidal crystal proteins of Bacillus thuringiensis
RT subsp. kurstaki possess different host range specificities.";
RL J. Bacteriol. 171:965-974(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-26.
RC STRAIN=HD-1, and HD-263;
RX PubMed=3121615; DOI=10.1016/s0021-9258(19)57428-2;
RA Donovan W.P., Dankocsik C.C., Gilbert M.P., Gawron-Burke M.C., Groat R.G.,
RA Carlton B.C.;
RT "Amino acid sequence and entomocidal activity of the P2 crystal protein. An
RT insect toxin from Bacillus thuringiensis var. kurstaki.";
RL J. Biol. Chem. 263:561-567(1988).
RN [3]
RP ERRATUM OF PUBMED:3121615, AND SEQUENCE REVISION.
RA Donovan W.P., Dankocsik C.C., Gilbert M.P., Gawron-Burke M.C., Groat R.G.,
RA Carlton B.C.;
RL J. Biol. Chem. 264:4740-4740(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11377201; DOI=10.1016/s0969-2126(01)00601-3;
RA Morse R.J., Yamamoto T., Stroud R.M.;
RT "Structure of Cry2Aa suggests an unexpected receptor binding epitope.";
RL Structure 9:409-417(2001).
CC -!- FUNCTION: Promotes colloidosmotic lysis by binding to the midgut
CC epithelial cells of both dipteran (Aedes aegypti) and lepidopteran
CC (Manduca sexta) larvae. {ECO:0000269|PubMed:2914879}.
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 -!- INDUCTION: Transcribed starting in early sporulation and into later
CC stages; not expressed during vegetative growth. Third gene in the orf1-
CC orf2-cry2Aa (cryB1) operon. {ECO:0000305|PubMed:2914879}.
CC -!- MISCELLANEOUS: Toxic segment of the protein is located in the N-
CC terminus.
CC -!- MISCELLANEOUS: Encoded on an unnamed 225 kb plasmid.
CC {ECO:0000269|PubMed:2914879}.
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; M23723; AAA83516.1; -; Genomic_DNA.
DR EMBL; M31738; AAA22335.1; -; Genomic_DNA.
DR PIR; C32053; C32053.
DR RefSeq; WP_001067062.1; NZ_PGEH01000148.1.
DR PDB; 1I5P; X-ray; 2.20 A; A=1-633.
DR PDBsum; 1I5P; -.
DR AlphaFoldDB; P0A377; -.
DR SMR; P0A377; -.
DR EvolutionaryTrace; P0A377; -.
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; IPR008979; Galactose-bd-like_sf.
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 Pfam; PF03944; Endotoxin_C; 1.
DR Pfam; PF09131; Endotoxin_mid; 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; Direct protein sequencing; Plasmid; Sporulation; Toxin;
KW Virulence.
FT CHAIN 1..633
FT /note="Pesticidal crystal protein Cry2Aa"
FT /id="PRO_0000174055"
FT VARIANT 1
FT /note="Missing (in 50% of the molecules)"
FT /evidence="ECO:0000269|PubMed:3121615"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 107..135
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 170..193
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 202..232
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:1I5P"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:1I5P"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 308..321
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 328..342
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1I5P"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:1I5P"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 422..432
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:1I5P"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 527..537
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 542..550
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 601..610
FT /evidence="ECO:0007829|PDB:1I5P"
FT STRAND 617..626
FT /evidence="ECO:0007829|PDB:1I5P"
SQ SEQUENCE 633 AA; 70852 MW; 15182F4C778E58A4 CRC64;
MNNVLNSGRT TICDAYNVVA HDPFSFEHKS LDTIQKEWME WKRTDHSLYV APVVGTVSSF
LLKKVGSLIG KRILSELWGI IFPSGSTNLM QDILRETEQF LNQRLNTDTL ARVNAELIGL
QANIREFNQQ VDNFLNPTQN PVPLSITSSV NTMQQLFLNR LPQFQIQGYQ LLLLPLFAQA
ANMHLSFIRD VILNADEWGI SAATLRTYRD YLRNYTRDYS NYCINTYQTA FRGLNTRLHD
MLEFRTYMFL NVFEYVSIWS LFKYQSLMVS SGANLYASGS GPQQTQSFTA QNWPFLYSLF
QVNSNYILSG ISGTRLSITF PNIGGLPGST TTHSLNSARV NYSGGVSSGL IGATNLNHNF
NCSTVLPPLS TPFVRSWLDS GTDREGVATS TNWQTESFQT TLSLRCGAFS ARGNSNYFPD
YFIRNISGVP LVIRNEDLTR PLHYNQIRNI ESPSGTPGGA RAYLVSVHNR KNNIYAANEN
GTMIHLAPED YTGFTISPIH ATQVNNQTRT FISEKFGNQG DSLRFEQSNT TARYTLRGNG
NSYNLYLRVS SIGNSTIRVT INGRVYTVSN VNTTTNNDGV NDNGARFSDI NIGNIVASDN
TNVTLDINVT LNSGTPFDLM NIMFVPTNLP PLY
