ID   CAPSD_BPPM2             Reviewed;         269 AA.
AC   P15794; Q9XJR7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   29-SEP-2021, entry version 54.
DE   RecName: Full=Major capsid protein P2;
DE            Short=Protein II;
GN   Name=II;
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 1-39.
RX   PubMed=964262; DOI=10.1111/j.1432-1033.1976.tb10772.x;
RA   Hinnen R., Chassin R., Schaefer R., Franklin R.M., Hitz H., Schaefer D.;
RT   "Structure and synthesis of a lipid-containing bacteriophage. Purification,
RT   chemical composition, and partial sequences of the structural proteins.";
RL   Eur. J. Biochem. 68:139-152(1976).
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   SUBUNIT, 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: Major capsid protein.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:12134022}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:12134022}.
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DR   EMBL; AF155037; AAD43549.1; -; Genomic_DNA.
DR   PIR; A12629; A12629.
DR   RefSeq; NP_049903.1; NC_000867.1.
DR   PDB; 2VVF; X-ray; 2.50 A; A/B/C/D/E/F=1-269.
DR   PDB; 2W0C; X-ray; 7.00 A; A/B/C/D/E/F/G/H/I/J=1-269.
DR   PDBsum; 2VVF; -.
DR   PDBsum; 2W0C; -.
DR   SMR; P15794; -.
DR   PRIDE; P15794; -.
DR   GeneID; 1262043; -.
DR   KEGG; vg:1262043; -.
DR   EvolutionaryTrace; P15794; -.
DR   Proteomes; UP000002136; Genome.
DR   GO; GO:0098017; C:viral capsid, major subunit; IDA:CACAO.
DR   InterPro; IPR041377; P2_N.
DR   Pfam; PF18628; P2_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing;
KW   Reference proteome; Virion.
FT   CHAIN           1..269
FT                   /note="Major capsid protein P2"
FT                   /id="PRO_0000089986"
FT   VARIANT         19
FT                   /note="C -> R"
FT   CONFLICT        9
FT                   /note="S -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="G -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19..20
FT                   /note="CS -> EP (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38
FT                   /note="G -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..6
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          25..39
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          44..51
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          54..61
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   HELIX           97..102
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          128..137
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          143..154
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          156..161
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          171..178
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          180..189
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          192..199
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   HELIX           200..209
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          218..223
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          242..250
FT                   /evidence="ECO:0007829|PDB:2VVF"
FT   STRAND          252..263
FT                   /evidence="ECO:0007829|PDB:2VVF"
SQ   SEQUENCE   269 AA;  30199 MW;  3CD9936A484BB1D0 CRC64;
     MRSFLNLNSI PNVAAGNSCS IKLPIGQTYE VIDLRYSGVT PSQIKNVRVE LDGRLLSTYK
     TLNDLILENT RHKRKIKAGV VSFHFVRPEM KGVNVTDLVQ QRMFALGTVG LTTCEIKFDI
     DEAAAGPKLS AIAQKSVGTA PSWLTMRRNF FKQLNNGTTE IADLPRPVGY RIAAIHIKAA
     GVDAVEFQID GTKWRDLLKK ADNDYILEQY GKAVLDNTYT IDFMLEGDVY QSVLLDQMIQ
     DLRLKIDSTM DEQAEIIVEY MGVWSRNGF