ID   P4_BPPM2                Reviewed;          40 AA.
AC   Q37958;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 59.
DE   RecName: Full=Protein P4;
DE   AltName: Full=Protein IV;
GN   Name=IV;
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=6518279; DOI=10.1007/bf01138171;
RA   Miller F.D., Winkfein R.J., Rattner J.B., van de Sande J.H.;
RT   "Sequence analysis of a PM2-DNA anti-Z-IgG-binding region.";
RL   Biosci. Rep. 4:885-895(1984).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION, AND 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   [5]
RP   PROTEIN SEQUENCE OF 1-10, AND 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).
CC   -!- FUNCTION: May interact with the viral DNA.
CC       {ECO:0000269|PubMed:7408847}.
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. Located partially in the inner leaflet of
CC       the bilayer. {ECO:0000305}.
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DR   EMBL; M26134; AAA32194.1; -; Genomic_DNA.
DR   EMBL; AF155037; AAD43551.1; -; Genomic_DNA.
DR   RefSeq; NP_049905.1; NC_000867.1.
DR   SMR; Q37958; -.
DR   GeneID; 1262045; -.
DR   KEGG; vg:1262045; -.
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   Capsid inner membrane protein; Direct protein sequencing; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..40
FT                   /note="Protein P4"
FT                   /id="PRO_0000339901"
FT   TRANSMEM        10..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   40 AA;  4389 MW;  B138B9941B1653B9 CRC64;
     MQKPSGKGLK YFAYGVAISA AGAILAEYVR DWMRKPKAKS