CR6AA_BACTU
ID CR6AA_BACTU Reviewed; 475 AA.
AC Q45757;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Pesticidal crystal protein Cry6Aa;
DE AltName: Full=Crystaline entomocidal protoxin;
DE Short=Crystal protein;
DE AltName: Full=Insecticidal delta-endotoxin CryVIA(a);
DE Flags: Fragment;
GN Name=cry6Aa; Synonyms=cryVIa, cryVIA(a);
OS Bacillus thuringiensis.
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-18245 / PS52A1;
RA Narva K.E., Schwab G.E., Galasan T., Payne J.M.;
RT "Gene encoding a nematode-active toxin cloned from a Bacillus thuringiensis
RT isolate.";
RL Patent number US5236843, 17-AUG-1993.
RN [2]
RP FUNCTION, AND INTERACTION WITH C.ELEGANS ASP-1.
RX PubMed=26795495; DOI=10.1371/journal.ppat.1005389;
RA Zhang F., Peng D., Cheng C., Zhou W., Ju S., Wan D., Yu Z., Shi J.,
RA Deng Y., Wang F., Ye X., Hu Z., Lin J., Ruan L., Sun M.;
RT "Bacillus thuringiensis Crystal Protein Cry6Aa Triggers Caenorhabditis
RT elegans Necrosis Pathway Mediated by Aspartic Protease (ASP-1).";
RL PLoS Pathog. 12:E1005389-E1005389(2016).
RN [3] {ECO:0007744|PDB:5KUC, ECO:0007744|PDB:5KUD}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP DISULFIDE BOND, AND MUTAGENESIS OF LEU-259.
RX PubMed=27576487; DOI=10.1186/s12915-016-0295-9;
RA Dementiev A., Board J., Sitaram A., Hey T., Kelker M.S., Xu X., Hu Y.,
RA Vidal-Quist C., Chikwana V., Griffin S., McCaskill D., Wang N.X.,
RA Hung S.C., Chan M.K., Lee M.M., Hughes J., Wegener A., Aroian R.V.,
RA Narva K.E., Berry C.;
RT "The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally
RT similar to HlyE-family alpha pore-forming toxins.";
RL BMC Biol. 14:71-71(2016).
RN [4] {ECO:0007744|PDB:5GHE}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-401.
RX PubMed=27381865; DOI=10.1016/j.bbrc.2016.07.002;
RA Huang J., Guan Z., Wan L., Zou T., Sun M.;
RT "Crystal structure of Cry6Aa: A novel nematicidal ClyA-type alpha-pore-
RT forming toxin from Bacillus thuringiensis.";
RL Biochem. Biophys. Res. Commun. 478:307-313(2016).
CC -!- FUNCTION: Pore-forming toxin with nematicidal activity
CC (PubMed:26795495, PubMed:27576487). In infected C.elegans, induces an
CC increase in intracellular Ca(2+) resulting in necrosis of host
CC intestinal cells (PubMed:26795495). Also, induces the expression of
CC aspartic protease asp-1 (PubMed:26795495).
CC {ECO:0000269|PubMed:26795495, ECO:0000269|PubMed:27576487}.
CC -!- SUBUNIT: Interacts with C.elegans aspartic protease asp-1; the
CC interaction prevents Cry6Aa proteolysis by host gut proteases.
CC {ECO:0000269|PubMed:26795495}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cell membrane
CC {ECO:0000305|PubMed:27576487}. Note=Probably secreted as a soluble
CC protein that then inserts into the host membrane and forms pores.
CC {ECO:0000305|PubMed:27576487}.
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 cry6A endotoxin family. {ECO:0000305}.
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DR EMBL; L07022; AAA22357.1; -; Genomic_DNA.
DR RefSeq; WP_043924592.1; NZ_LDFL01000446.1.
DR PDB; 5GHE; X-ray; 1.90 A; A=1-401.
DR PDB; 5KUC; X-ray; 2.00 A; A=1-475.
DR PDB; 5KUD; X-ray; 2.70 A; A=1-475.
DR PDBsum; 5GHE; -.
DR PDBsum; 5KUC; -.
DR PDBsum; 5KUD; -.
DR AlphaFoldDB; Q45757; -.
DR SMR; Q45757; -.
DR TCDB; 1.C.41.2.1; the tripartite haemolysin bl (hbl) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Host cell membrane; Host membrane; Membrane;
KW Secreted; Sporulation; Toxin; Virulence.
FT CHAIN 1..>475
FT /note="Pesticidal crystal protein Cry6Aa"
FT /id="PRO_0000174070"
FT REGION 250..268
FT /note="Potential transmembrane region for insertion into
FT the host cell membrane"
FT /evidence="ECO:0000303|PubMed:27576487"
FT DISULFID 88..451
FT /evidence="ECO:0000269|PubMed:27576487,
FT ECO:0007744|PDB:5KUC, ECO:0007744|PDB:5KUD"
FT DISULFID 402..404
FT /evidence="ECO:0000303|PubMed:27576487"
FT MUTAGEN 259
FT /note="L->D: Loss of nematicidal activity."
FT /evidence="ECO:0000269|PubMed:27576487"
FT NON_TER 475
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:5GHE"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:5GHE"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:5GHE"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5KUC"
FT HELIX 148..188
FT /evidence="ECO:0007829|PDB:5GHE"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:5GHE"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5KUC"
FT HELIX 220..241
FT /evidence="ECO:0007829|PDB:5GHE"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 271..288
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 292..343
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:5GHE"
FT HELIX 357..383
FT /evidence="ECO:0007829|PDB:5GHE"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:5KUC"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:5KUC"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:5KUC"
SQ SEQUENCE 475 AA; 54075 MW; 8ADAF318D412EBCB CRC64;
MIIDSKTTLP RHSLIHTIKL NSNKKYGPGD MTNGNQFIIS KQEWATIGAY IQTGLGLPVN
EQQLRTHVNL SQDISIPSDF SQLYDVYCSD KTSAEWWNKN LYPLIIKSAN DIASYGFKVA
GDPSIKKDGY FKKLQDELDN IVDNNSDDDA IAKAIKDFKA RCGILIKEAK QYEEAAKNIV
TSLDQFLHGD QKKLEGVINI QKRLKEVQTA LNQAHGESSP AHKELLEKVK NLKTTLERTI
KAEQDLEKKV EYSFLLGPLL GFVVYEILEN TAVQHIKNQI DEIKKQLDSA QHDLDRDVKI
IGMLNSINTD IDNLYSQGQE AIKVFQKLQG IWATIGAQIE NLRTTSLQEV QDSDDADEIQ
IELEDASDAW LVVAQEARDF TLNAYSTNSR QNLPINVISD SCNCSTTNMT SNQYSNPTTN
MTSNQYMISH EYTSLPNNFM LSRNSNLEYK CPENNFMIYW YNNSDWYNNS DWYNN
