KP6T_UMV6
ID KP6T_UMV6 Reviewed; 219 AA.
AC P16948; Q02118; Q02120; Q08941;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 29-SEP-2021, entry version 102.
DE RecName: Full=KP6 killer toxin;
DE AltName: Full=Killer protein 6;
DE Contains:
DE RecName: Full=KP6 killer toxin subunit alpha;
DE AltName: Full=VP10;
DE Contains:
DE RecName: Full=KP6 killer toxin subunit beta;
DE AltName: Full=VP12.5;
DE Flags: Precursor;
OS Ustilago maydis P6 virus (UmV6) (UmV-P6).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC Ghabrivirales; Totiviridae; Totivirus.
OX NCBI_TaxID=11010;
OH NCBI_TaxID=5270; Ustilago maydis (Corn smut fungus).
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 28-61 AND 139-166.
RX PubMed=2181272; DOI=10.1128/mcb.10.4.1373-1381.1990;
RA Tao J., Ginsberg I., Banerjee N., Held W., Koltin Y., Bruenn J.A.;
RT "Ustilago maydis KP6 killer toxin: structure, expression in Saccharomyces
RT cerevisiae, and relationship to other cellular toxins.";
RL Mol. Cell. Biol. 10:1373-1381(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NK13, and NK3;
RX PubMed=8479428; DOI=10.1007/bf00279552;
RA Tao J., Ginzberg I., Koltin Y., Bruenn J.A.;
RT "Mutants of Ustilago maydis defective in production of one of two
RT polypeptides of KP6 toxin from the preprotoxin.";
RL Mol. Gen. Genet. 238:234-240(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-106.
RX PubMed=10400668; DOI=10.1074/jbc.274.29.20425;
RA Li N., Erman M., Pangborn W., Duax W.L., Park C.M., Bruenn J., Ghosh D.;
RT "Structure of Ustilago maydis killer toxin KP6 alpha-subunit. A multimeric
RT assembly with a central pore.";
RL J. Biol. Chem. 274:20425-20431(1999).
CC -!- FUNCTION: This protein is lethal to sensitive cells of the same or
CC related species. The KP6 alpha subunit is known to recognize some
CC cellular receptors before interaction of the complex with KP6 beta,
CC precipitating cell death.
CC -!- SUBUNIT: Heterodimer of two small polypeptides that are not covalently
CC linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: The KP6 toxin polypeptides interact with the cell
CC independently, as monomers.
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DR EMBL; M27418; AAA47957.1; -; Genomic_RNA.
DR EMBL; S59589; AAB26391.1; -; Other_RNA.
DR EMBL; S59590; AAB26392.1; -; Other_RNA.
DR PIR; A34778; A34778.
DR PDB; 1KP6; X-ray; 1.80 A; A=28-106.
DR PDB; 4GVB; X-ray; 1.80 A; A=28-107, B=139-219.
DR PDBsum; 1KP6; -.
DR PDBsum; 4GVB; -.
DR SMR; P16948; -.
DR EvolutionaryTrace; P16948; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..19
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:2181272"
FT /id="PRO_0000041339"
FT CHAIN 28..105
FT /note="KP6 killer toxin subunit alpha"
FT /id="PRO_0000041340"
FT PROPEP 106..138
FT /evidence="ECO:0000269|PubMed:2181272"
FT /id="PRO_0000041341"
FT CHAIN 139..219
FT /note="KP6 killer toxin subunit beta"
FT /id="PRO_0000041342"
FT REGION 120..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 32..39
FT DISULFID 43..101
FT DISULFID 45..92
FT DISULFID 62..78
FT VARIANT 78
FT /note="C -> R (in strain: NK3)"
FT VARIANT 163
FT /note="T -> P (in strain: NK13)"
FT VARIANT 180
FT /note="K -> R (in strain: NK13)"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1KP6"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1KP6"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1KP6"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:1KP6"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1KP6"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1KP6"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1KP6"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1KP6"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1KP6"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1KP6"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:4GVB"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4GVB"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:4GVB"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4GVB"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:4GVB"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:4GVB"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4GVB"
SQ SEQUENCE 219 AA; 24071 MW; 9E6AD13DF7EC032F CRC64;
MLIFSVLMYL GLLLAGASAL PNGLSPRNNA FCAGFGLSCK WECWCTAHGT GNELRYATAA
GCGDHLSKSY YDARAGHCLF SDDLRNQFYS HCSSLNNNMS CRSLSKRTIQ DSATDTVDLG
AELHRDDPPP TASDIGKRGK RPRPVMCQCV DTTNGGVRLD AVTRAACSID SFIDGYYTEK
DGFCRAKYSW DLFTSGQFYQ ACLRYSHAGT NCQPDPQYE
