CAPSD_BPPRD
ID CAPSD_BPPRD Reviewed; 395 AA.
AC P22535; Q3T4N2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Major capsid protein P3;
DE AltName: Full=Protein P3;
GN Name=III;
OS Enterobacteria phage PRD1 (Bacteriophage PRD1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Kalamavirales; Tectiviridae; Alphatectivirus.
OX NCBI_TaxID=10658;
OH NCBI_TaxID=471; Acinetobacter calcoaceticus.
OH NCBI_TaxID=562; Escherichia coli.
OH NCBI_TaxID=584; Proteus mirabilis.
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
OH NCBI_TaxID=294; Pseudomonas fluorescens.
OH NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
OH NCBI_TaxID=90371; Salmonella typhimurium.
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=2196741; DOI=10.1016/0042-6822(90)90508-o;
RA Bamford J.K.H., Bamford D.H.;
RT "Capsomer proteins of bacteriophage PRD1, a bacterial virus with a
RT membrane.";
RL Virology 177:445-451(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
RA Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
RA Bamford D.H., Bamford J.K.H.;
RT "A snapshot of viral evolution from genome analysis of the tectiviridae
RT family.";
RL J. Mol. Biol. 350:427-440(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=8450547; DOI=10.1006/jmbi.1993.1148;
RA Stewart P.L., Ghosh S., Bamford D.H., Burnett R.M.;
RT "Crystallization of the major coat protein of PRD1, a bacteriophage with an
RT internal membrane.";
RL J. Mol. Biol. 230:349-352(1993).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (1.65 ANGSTROMS).
RX PubMed=11752778; DOI=10.1107/s0907444901017279;
RA Benson S.D., Bamford J.K.H., Bamford D.H., Burnett R.M.;
RT "The X-ray crystal structure of P3, the major coat protein of the lipid-
RT containing bacteriophage PRD1, at 1.65 A resolution.";
RL Acta Crystallogr. D 58:39-59(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS).
RX PubMed=15525981; DOI=10.1038/nature03056;
RA Abrescia N.G.A., Cockburn J.J.B., Grimes J.M., Sutton G.C., Diprose J.M.,
RA Butcher S.J., Fuller S.D., San Martin C., Burnett R.M., Stuart D.I.,
RA Bamford D.H., Bamford J.K.H.;
RT "Insights into assembly from structural analysis of bacteriophage PRD1.";
RL Nature 432:68-74(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS).
RX PubMed=15525993; DOI=10.1038/nature03053;
RA Cockburn J.J., Abrescia N.G., Grimes J.M., Sutton G.C., Diprose J.M.,
RA Benevides J.M., Thomas G.J. Jr., Bamford J.K.H., Bamford D.H., Stuart D.I.;
RT "Membrane structure and interactions with protein and DNA in bacteriophage
RT PRD1.";
RL Nature 432:122-125(2004).
CC -!- FUNCTION: Major capsid protein self-assembles to form an icosahedral
CC capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and
CC consisting of 240 capsid proteins trimers. The capsid encapsulates an
CC inner membrane and the genomic dsDNA genome. The major coat protein P3
CC and two assembly factors (P10 and P17) are needed during the assembly
CC of the virus particle inside the host cell, when the capsid protein
CC multimers are capable of enclosing the host-derived membrane,
CC containing the virus-encoded membrane-associated proteins.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Virion.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1hb9";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1gw7";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of SUS607 mutant;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1gw8";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral virus
CC capsid P3-shell structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1hb5";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of SUS1 mutant;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1hb7";
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DR EMBL; AY848689; AAX45916.1; -; Genomic_DNA.
DR EMBL; M55567; AAA32445.1; -; Genomic_DNA.
DR PIR; A46345; A46345.
DR RefSeq; NP_040692.1; NC_001421.2.
DR PDB; 1CJD; X-ray; 1.85 A; A/B/C=2-395.
DR PDB; 1GW7; EM; 13.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-395.
DR PDB; 1GW8; EM; 13.30 A; A/B/C/D/E/F/G/H/I/J/K/L=2-395.
DR PDB; 1HB5; EM; 12.00 A; A/B/C/D/E/F/G/H/I=2-395.
DR PDB; 1HB7; EM; 14.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-395.
DR PDB; 1HB9; EM; 25.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-395.
DR PDB; 1HQN; X-ray; 2.20 A; A/B/C=2-395.
DR PDB; 1HX6; X-ray; 1.65 A; A/B/C=2-395.
DR PDB; 1W8X; X-ray; 4.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-395.
DR PDBsum; 1CJD; -.
DR PDBsum; 1GW7; -.
DR PDBsum; 1GW8; -.
DR PDBsum; 1HB5; -.
DR PDBsum; 1HB7; -.
DR PDBsum; 1HB9; -.
DR PDBsum; 1HQN; -.
DR PDBsum; 1HX6; -.
DR PDBsum; 1W8X; -.
DR SMR; P22535; -.
DR PRIDE; P22535; -.
DR EvolutionaryTrace; P22535; -.
DR Proteomes; UP000002143; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 2.70.9.30; -; 1.
DR InterPro; IPR015108; Phage_PRD1_P3.
DR InterPro; IPR016115; Phage_PRD1_P3_N.
DR InterPro; IPR029053; Viral_coat.
DR InterPro; IPR016112; VP_dsDNA_II.
DR Pfam; PF09018; Phage_Capsid_P3; 1.
DR SUPFAM; SSF49749; SSF49749; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing;
KW Reference proteome; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:2196741"
FT CHAIN 2..395
FT /note="Major capsid protein P3"
FT /id="PRO_0000165345"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 35..47
FT /evidence="ECO:0007829|PDB:1HX6"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 63..78
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1HX6"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1HX6"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 159..175
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1HX6"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1HX6"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 223..239
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1HX6"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:1HX6"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1HX6"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1HX6"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:1CJD"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:1HX6"
FT STRAND 371..382
FT /evidence="ECO:0007829|PDB:1HX6"
SQ SEQUENCE 395 AA; 43448 MW; 44731365E74C4375 CRC64;
MAQVQQLTPA QQAALRNQQA MAANLQARQI VLQQSYPVIQ QVETQTFDPA NRSVFDVTPA
NVGIVKGFLV KVTAAITNNH ATEAVALTDF GPANLVQRVI YYDPDNQRHT ETSGWHLHFV
NTAKQGAPFL SSMVTDSPIK YGDVMNVIDA PATIAAGATG ELTMYYWVPL AYSETDLTGA
VLANVPQSKQ RLKLEFANNN TAFAAVGANP LEAIYQGAGA ADCEFEEISY TVYQSYLDQL
PVGQNGYILP LIDLSTLYNL ENSAQAGLTP NVDFVVQYAN LYRYLSTIAV FDNGGSFNAG
TDINYLSQRT ANFSDTRKLD PKTWAAQTRR RIATDFPKGV YYCDNRDKPI YTLQYGNVGF
VVNPKTVNQN ARLLMGYEYF TSRTELVNAG TISTT
