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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
 
 
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