BUBL_PENBR
ID BUBL_PENBR Reviewed; 64 AA.
AC P83799;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Bubble protein;
OS Penicillium brevicompactum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5074;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=14747700; DOI=10.1107/s0907444903025927;
RA Olsen J.G., Flensburg C., Olsen O., Bricogne G., Henriksen A.;
RT "Solving the structure of the bubble protein using the anomalous sulfur
RT signal from single-crystal in-house Cu Kalpha diffraction data only.";
RL Acta Crystallogr. D 60:250-255(2004).
CC -!- FUNCTION: May act as a toxin. May recognize a molecule or part of a
CC molecule with a negatively charged surface potential.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR PDB; 1UOY; X-ray; 1.50 A; A=1-64.
DR PDBsum; 1UOY; -.
DR AlphaFoldDB; P83799; -.
DR SMR; P83799; -.
DR EvolutionaryTrace; P83799; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR015308; Bubble.
DR InterPro; IPR036334; Bubble_sf.
DR Pfam; PF09227; DUF1962; 1.
DR SUPFAM; SSF103565; SSF103565; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Secreted.
FT CHAIN 1..64
FT /note="Bubble protein"
FT /id="PRO_0000065011"
FT DISULFID 3..30
FT DISULFID 18..38
FT DISULFID 28..54
FT DISULFID 49..64
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1UOY"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1UOY"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1UOY"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1UOY"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1UOY"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1UOY"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1UOY"
SQ SEQUENCE 64 AA; 6570 MW; 76B05414181FF06E CRC64;
DTCGSGYNVD QRRTNSGCKA GNGDRHFCGC DRTGVVECKG GKWTEVQDCG SSSCKGTSNG
GATC