KP4T_UMV4
ID KP4T_UMV4 Reviewed; 127 AA.
AC Q90121;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 87.
DE RecName: Full=KP4 killer toxin;
DE AltName: Full=Fungal toxin KP4;
DE AltName: Full=Killer protein 4;
DE Flags: Precursor;
GN Name=M2A;
OS Ustilago maydis P4 virus (UmV4) (UmV-P4).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC Ghabrivirales; Totiviridae; Totivirus.
OX NCBI_TaxID=11009;
OH NCBI_TaxID=5270; Ustilago maydis (Corn smut fungus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 23-79 AND 124-127,
RP AND MASS SPECTROMETRY.
RC STRAIN=77;
RX PubMed=8145639; DOI=10.1111/j.1365-2958.1994.tb00297.x;
RA Park C.-M., Bruenn J.A., Ganesa C., Flurkey W.F., Bozarth R.F., Koltin Y.;
RT "Structure and heterologous expression of the Ustilago maydis viral toxin
RT KP4.";
RL Mol. Microbiol. 11:155-164(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=M2B;
RA Gu F., Khimani A.K., Flurkey W.F., Bozarth R.F., Smith T.J., Rane S.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 23-52.
RX PubMed=1897946; DOI=10.1016/0003-9861(91)90027-g;
RA Ganesa C., Flurkey W.H., Randhawa Z.I., Bozarth R.F.;
RT "Ustilago maydis virus P4 killer toxin: characterization, partial amino
RT terminus sequence, and evidence for glycosylation.";
RL Arch. Biochem. Biophys. 286:195-200(1991).
RN [4]
RP FUNCTION.
RX PubMed=11532143; DOI=10.1046/j.1365-2958.2001.02554.x;
RA Gage M.J., Bruenn J., Fischer M., Sanders D., Smith T.J.;
RT "KP4 fungal toxin inhibits growth in Ustilago maydis by blocking calcium
RT uptake.";
RL Mol. Microbiol. 41:775-785(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=7582897; DOI=10.1016/s0969-2126(01)00215-5;
RA Gu F., Khimani A., Rane S.G., Flurkey W.H., Bozarth R.F., Smith T.J.;
RT "Structure and function of a virally encoded fungal toxin from Ustilago
RT maydis: a fungal and mammalian Ca2+ channel inhibitor.";
RL Structure 3:805-814(1995).
CC -!- FUNCTION: This protein is lethal to sensitive cells of the same or
CC related species. It specifically inhibits voltage-gated calcium
CC channels. It inhibits cell growth and division by blocking calcium
CC import. {ECO:0000269|PubMed:11532143}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: Mass=11045; Mass_error=11; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8145639};
CC -!- BIOTECHNOLOGY: The KP4 toxin expressed in transgenic plant can render
CC them resistant to KP4-susceptible fungal pathogens such as grass smut
CC fungi. Successful tests have been made in tobacco and wheat.
CC -!- CAUTION: Was originally thought to be glycosylated, but this does not
CC seem to be the case according to PubMed:8145639.
CC {ECO:0000305|PubMed:1897946}.
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DR EMBL; L12226; AAA89185.1; -; Genomic_RNA.
DR EMBL; U25179; AAA75041.1; -; Genomic_RNA.
DR PIR; S40034; S40034.
DR PDB; 1KPT; X-ray; 1.75 A; A/B=23-127.
DR PDBsum; 1KPT; -.
DR SMR; Q90121; -.
DR EvolutionaryTrace; Q90121; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR015131; Killer_tox_Kp4.
DR InterPro; IPR011329; Killer_tox_Kp4/SMK.
DR Pfam; PF09044; Kp4; 1.
DR SUPFAM; SSF55221; SSF55221; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1897946,
FT ECO:0000269|PubMed:8145639"
FT CHAIN 23..127
FT /note="KP4 killer toxin"
FT /id="PRO_0000041338"
FT DISULFID 27..100
FT DISULFID 33..103
FT DISULFID 49..89
FT DISULFID 57..82
FT DISULFID 66..127
FT CONFLICT 56
FT /note="W -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="C -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="G -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="A -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="T -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:1KPT"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1KPT"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1KPT"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1KPT"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1KPT"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1KPT"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1KPT"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1KPT"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1KPT"
SQ SEQUENCE 127 AA; 13489 MW; 34CAA729C9A63E1E CRC64;
MQIINVVYSF LFAAAMLPVV HSLGINCRGS SQCGLSGGNL MVRIRDQACG NQGQTWCPGE
RRAKVCGTGN SISAYVQSTN NCISGTEACR HLTNLVNHGC RVCGSDPLYA GNDVSRGQLT
VNYVNSC
