P3_BPPM2
ID P3_BPPM2 Reviewed; 104 AA.
AC Q9XJR6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 29-SEP-2021, entry version 58.
DE RecName: Full=Protein P3;
DE AltName: Full=Protein III;
GN Name=III;
OS Pseudoalteromonas phage PM2 (Bacteriophage PM2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Vinavirales; Corticoviridae; Corticovirus.
OX NCBI_TaxID=10661;
OH NCBI_TaxID=28107; Pseudoalteromonas espejiana.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10502514; DOI=10.1006/viro.1999.9837;
RA Maennistoe R.H., Kivelae H.M., Paulin L., Bamford D.H., Bamford J.K.;
RT "The complete genome sequence of PM2, the first lipid-containing bacterial
RT virus to be isolated.";
RL Virology 262:355-363(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=10502515; DOI=10.1006/viro.1999.9838;
RA Kivelae H.M., Maennistoe R.H., Kalkkinen N., Bamford D.H.;
RT "Purification and protein composition of PM2, the first lipid-containing
RT bacterial virus to be isolated.";
RL Virology 262:364-374(1999).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=7408847; DOI=10.1111/j.1432-1033.1980.tb04712.x;
RA Satake H., Akutsu H., Kania M., Franklin R.M.;
RT "Structure and synthesis of a lipid-containing bacteriophage. Studies on
RT the structure of the bacteriophage PM2 nucleocapsid.";
RL Eur. J. Biochem. 108:193-201(1980).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12134022; DOI=10.1128/jvi.76.16.8169-8178.2002;
RA Kivelae H.M., Kalkkinen N., Bamford D.H.;
RT "Bacteriophage PM2 has a protein capsid surrounding a spherical
RT proteinaceous lipid core.";
RL J. Virol. 76:8169-8178(2002).
RN [5] {ECO:0007744|PDB:2W0C}
RP X-RAY CRYSTALLOGRAPHY (7.00 ANGSTROMS), SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18775333; DOI=10.1016/j.molcel.2008.06.026;
RA Abrescia N.G., Grimes J.M., Kivela H.M., Assenberg R., Sutton G.C.,
RA Butcher S.J., Bamford J.K., Bamford D.H., Stuart D.I.;
RT "Insights into virus evolution and membrane biogenesis from the structure
RT of the marine lipid-containing bacteriophage PM2.";
RL Mol. Cell 31:749-761(2008).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18775333}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:12134022,
CC ECO:0000305|PubMed:7408847}; Single-pass membrane protein
CC {ECO:0000305|PubMed:12134022, ECO:0000305|PubMed:7408847}. Note=Part of
CC the capsid inner membrane. Deeply embedded in the lipid bilayer. About
CC 20% of the molecule extends to the exterior.
CC {ECO:0000305|PubMed:18775333}.
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DR EMBL; AF155037; AAD43550.1; -; Genomic_DNA.
DR RefSeq; NP_049904.1; NC_000867.1.
DR PDB; 2W0C; X-ray; 7.00 A; P/Q/R/S=1-104.
DR PDBsum; 2W0C; -.
DR SMR; Q9XJR6; -.
DR GeneID; 1262044; -.
DR KEGG; vg:1262044; -.
DR EvolutionaryTrace; Q9XJR6; -.
DR Proteomes; UP000002136; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039641; C:viral inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IDA:CACAO.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid inner membrane protein; Direct protein sequencing;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; Virion.
FT CHAIN 1..104
FT /note="Protein P3"
FT /id="PRO_0000339900"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 104 AA; 10758 MW; 66C9DB3A77E93DFD CRC64;
MNTSVPTSVP TNQSVWGNVS TGLDALISGW ARVEQIKAAK ASTGQGRVEQ AMTPELDNGA
AVVVEAPKKA AQPSETLVFG VPQKTLLLGF GGLLVLGLVM RGNK