CR1AA_BACTS
ID CR1AA_BACTS Reviewed; 934 AA.
AC P0A369; P02965; P09664; P09665; P16478; Q9RED5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Pesticidal crystal protein Cry1Aa;
DE AltName: Full=133 kDa crystal protein;
DE AltName: Full=Crystaline entomocidal protoxin;
DE AltName: Full=Insecticidal delta-endotoxin CryIA(a);
DE Flags: Fragment;
GN Name=cry1Aa; Synonyms=cry-1-1, cry1A(a), cryA, crybns3-1, cryIA(a), icp;
OS Bacillus thuringiensis subsp. sotto.
OG Plasmid 68 Kb.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29340;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989108; DOI=10.1016/0378-1119(85)90133-7;
RA Shibano Y., Yamagata A., Nakamura N., Iizuka T., Sugisaki H., Takanami M.;
RT "Nucleotide sequence coding for the insecticidal fragment of the Bacillus
RT thuringiensis crystal protein.";
RL Gene 34:243-251(1985).
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; M10917; AAA22552.1; -; Genomic_DNA.
DR AlphaFoldDB; P0A369; -.
DR SMR; P0A369; -.
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 2: Evidence at transcript level;
KW Plasmid; Sporulation; Toxin; Virulence.
FT CHAIN 1..>934
FT /note="Pesticidal crystal protein Cry1Aa"
FT /id="PRO_0000174020"
FT NON_TER 934
SQ SEQUENCE 934 AA; 105673 MW; 961CEC04F299EBB3 CRC64;
MDNNPNINEC IPYNCLSNPE VEVLGGERIE TGYTPIDISL SLTQFLLSEF VPGAGFVLGL
VDIIWGIFGP SQWDAFLVQI EQLINQRIEE FARNQAISRL EGLSNLYQIY AESFREWEAD
PTNPALREEM RIQFNDMNSA LTTAIPLFAV QNYQVPLLSV YVQAANLHLS VLRDVSVFGQ
RWGFDAATIN SRYNDLTRLI GNYTDYAVRW YNTGLERVWG PDSRDWVRYN QFRRELTLTV
LDIVALFSNY DSRRYPIRTV SQLTREIYTN PVLENFDGSF RGMAQRIEQN IRQPHLMDIL
NRITIYTDVH RGFNYWSGHQ ITASPVGFSG PEFAFPLFGN AGNAAPPVLV SLTGLGIFRT
LSSPLYRRII LGSGPNNQEL FVLDGTEFSF ASLTTNLPST IYRQRGTVDS LDVIPPQDNS
VPPRAGFSHR LSHVTMLSQA AGAVYTLRAP TFSWQHRSAE FNNIIPSSQI TQIPLTKSTN
LGSGTSVVKG PGFTGGDILR RTSPGQISTL RVNITAPLSQ RYRVRIRYAS TTNLQFHTSI
DGRPINQGNF SATMSSGSNL QSGSFRTVGF TTPFNFSNGS SVFTLSAHVF NSGNEVYIDR
IEFVPAEVTF EAEYDLERAQ KAVNELFTSS NQIGLKTDVT DYHIDQVSNL VECLSDEFCL
DEKQELSEKV KHAKRLSDER NLLQDPNFRG INRQLDRGWR GSTDITIQGG DDVFKENYVT
LLGTFDECYP TYLYQKIDES KLKAYTRYQL RGYIEDSQDL EIYLIRYNAK HETVNVPGTG
SLWPLSAQSP IGKCGEPNRC APHLEWNPDL DCSCRDGEKC AHHSHHFSLD IDVGCTDLNE
DLGVWVIFKI KTQDGHARLG NLEFLEEKPL VGEALARVKR AEKKWRDKRE KLEWETNIVY
KEAKESVDAL FVNSQYDRLQ ADTNIAMIHA ADKR