DEF_PENBA
ID DEF_PENBA Reviewed; 54 AA.
AC P56552;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Defensin-like protein;
DE AltName: Full=Brazzein {ECO:0000303|PubMed:7957951};
OS Pentadiplandra brazzeana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Pentadiplandraceae; Pentadiplandra.
OX NCBI_TaxID=43545;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Fruit;
RX PubMed=7957951; DOI=10.1016/0014-5793(94)01184-2;
RA Ming D., Hellekant G.;
RT "Brazzein, a new high-potency thermostable sweet protein from
RT Pentadiplandra brazzeana B.";
RL FEBS Lett. 355:106-108(1994).
RN [2]
RP FUNCTION.
RX PubMed=15118082; DOI=10.1073/pnas.0401567101;
RA Yount N.Y., Yeaman M.R.;
RT "Multidimensional signatures in antimicrobial peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7363-7368(2004).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=9628478; DOI=10.1038/nsb0698-427;
RA Caldwell J.E., Abildgaard F., Dzakula Z., Ming D., Hellekant G.,
RA Markley J.L.;
RT "Solution structure of the thermostable sweet-tasting protein brazzein.";
RL Nat. Struct. Biol. 5:427-431(1998).
CC -!- FUNCTION: Taste-modifying protein; sweet-tasting. It is 2000 sweeter
CC than sucrose on a molar basis. {ECO:0000269|PubMed:15118082}.
CC -!- FUNCTION: Has a pH-specific antimicrobial activity against bacteria
CC (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.
CC {ECO:0000269|PubMed:15118082}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the DEFL 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 PIR; S51208; S51208.
DR PDB; 1BRZ; NMR; -; A=2-54.
DR PDB; 2BRZ; NMR; -; A=2-54.
DR PDB; 2KGQ; NMR; -; A=2-54.
DR PDB; 2KYQ; NMR; -; A=3-54.
DR PDB; 2LY5; NMR; -; A=2-54.
DR PDB; 2LY6; NMR; -; A=2-54.
DR PDB; 2N66; NMR; -; A=1-54.
DR PDB; 2N69; NMR; -; A=1-54.
DR PDB; 4HE7; X-ray; 1.80 A; A=1-54.
DR PDBsum; 1BRZ; -.
DR PDBsum; 2BRZ; -.
DR PDBsum; 2KGQ; -.
DR PDBsum; 2KYQ; -.
DR PDBsum; 2LY5; -.
DR PDBsum; 2LY6; -.
DR PDBsum; 2N66; -.
DR PDBsum; 2N69; -.
DR PDBsum; 4HE7; -.
DR AlphaFoldDB; P56552; -.
DR BMRB; P56552; -.
DR SMR; P56552; -.
DR TCDB; 1.C.45.4.2; the plant defensin (plant defensin) family.
DR EvolutionaryTrace; P56552; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Fungicide; Pyrrolidone carboxylic acid; Secreted;
KW Taste-modifying protein.
FT CHAIN 1..54
FT /note="Defensin-like protein"
FT /id="PRO_0000221427"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:7957951"
FT DISULFID 4..52
FT DISULFID 16..37
FT DISULFID 22..47
FT DISULFID 26..49
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4HE7"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:4HE7"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1BRZ"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:4HE7"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:4HE7"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2BRZ"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:4HE7"
SQ SEQUENCE 54 AA; 6498 MW; 5BAB4D7215291252 CRC64;
QDKCKKVYEN YPVSKCQLAN QCNYDCKLDK HARSGECFYD EKRNLQCICD YCEY
