ID   SCAFD_BPPHS             Reviewed;         152 AA.
AC   P69486; P03637;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-JUN-2021, entry version 87.
DE   RecName: Full=External scaffolding protein D;
DE   AltName: Full=Scaffolding protein D;
DE            Short=GPD;
GN   Name=D;
OS   Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus.
OX   NCBI_TaxID=1217068;
OH   NCBI_TaxID=498388; Escherichia coli C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=870828; DOI=10.1038/265687a0;
RA   Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C.,
RA   Hutchison C.A. III, Slocombe P.M., Smith M.;
RT   "Nucleotide sequence of bacteriophage phi X174 DNA.";
RL   Nature 265:687-695(1977).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11; 13-20;
RP   25-58; 61-93; 95-123 AND 125-152.
RX   PubMed=1004533; DOI=10.1038/264034a0;
RA   Barrell B.G., Air G.M., Hutchison C.A. III;
RT   "Overlapping genes in bacteriophage phiX174.";
RL   Nature 264:34-41(1976).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX   PubMed=2963134; DOI=10.1016/0022-2836(87)90203-8;
RA   Buckley K.J., Hayashi M.;
RT   "Role of premature translational termination in the regulation of
RT   expression of the phi X174 lysis gene.";
RL   J. Mol. Biol. 198:599-607(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-9, AND IDENTIFICATION.
RX   PubMed=1255852; DOI=10.1128/jvi.17.3.1027-1037.1976;
RA   Farber M.B.;
RT   "Purification and properties of bacteriophage phi X 174 gene D product.";
RL   J. Virol. 17:1027-1037(1976).
RN   [5]
RP   FUNCTION, AND PROCAPSID STRUCTURE.
RX   PubMed=159449; DOI=10.1073/pnas.76.10.4877;
RA   Mukai R., Hamatake R.K., Hayashi M.;
RT   "Isolation and identification of bacteriophage phi X174 prohead.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:4877-4881(1979).
RN   [6]
RP   MUTAGENESIS OF GLY-61.
RX   PubMed=12788631; DOI=10.1016/s0042-6822(03)00076-x;
RA   Burch A.D., Fane B.A.;
RT   "Genetic analyses of putative conformation switching and cross-species
RT   inhibitory domains in Microviridae external scaffolding proteins.";
RL   Virology 310:64-71(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=15890913; DOI=10.1128/jvi.79.11.6751-6756.2005;
RA   Uchiyama A., Fane B.A.;
RT   "Identification of an interacting coat-external scaffolding protein domain
RT   required for both the initiation of phiX174 procapsid morphogenesis and the
RT   completion of DNA packaging.";
RL   J. Virol. 79:6751-6756(2005).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND SUBUNIT.
RX   PubMed=9305849; DOI=10.1038/38537;
RA   Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A.,
RA   Rossmann M.G.;
RT   "Structure of a viral procapsid with molecular scaffolding.";
RL   Nature 389:308-313(1997).
CC   -!- FUNCTION: Assembles the procapsid by joining twelve 12S pre-assembly
CC       complex into a T=1 icosahedral particle, called 108S procapsid. Ten
CC       proteins D bind each 12S complex, which are formed by three pentamers
CC       of F, G, B protein and a H protein. The scaffolding protein is released
CC       from the provirion after genome packaging to form the mature virion.
CC       {ECO:0000269|PubMed:15890913, ECO:0000269|PubMed:159449}.
CC   -!- SUBUNIT: Component of the procapsid particle composed of 60 copies of
CC       the internally located B, 240 copies of the external scaffolding
CC       protein D, 60 copies of each of the viral structural proteins F and G,
CC       and 12 copies of protein H. {ECO:0000269|PubMed:9305849}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC   -!- SIMILARITY: Belongs to the microvirus D protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J02482; AAA32575.1; -; Genomic_DNA.
DR   EMBL; X07809; CAA30667.1; -; Genomic_DNA.
DR   PIR; A04245; ZDBPF4.
DR   PDB; 1AL0; X-ray; 3.50 A; 1/2/3/4=1-152.
DR   PDB; 1CD3; X-ray; 3.50 A; 1/2/3/4=1-152.
DR   PDB; 1M0F; EM; 16.00 A; 1/2/3/4=1-152.
DR   PDB; 1TX9; X-ray; 3.31 A; A/B=2-152.
DR   PDBsum; 1AL0; -.
DR   PDBsum; 1CD3; -.
DR   PDBsum; 1M0F; -.
DR   PDBsum; 1TX9; -.
DR   SMR; P69486; -.
DR   EvolutionaryTrace; P69486; -.
DR   Proteomes; UP000005893; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046797; P:viral procapsid maturation; IEA:InterPro.
DR   Gene3D; 1.10.1850.10; -; 1.
DR   InterPro; IPR004196; Scaffold_D.
DR   InterPro; IPR036632; Scaffold_D_sf.
DR   Pfam; PF02925; gpD; 1.
DR   SUPFAM; SSF48045; SSF48045; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Host cytoplasm;
KW   Reference proteome; Viral capsid assembly; Viral release from host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000269|PubMed:1004533,
FT                   ECO:0000269|PubMed:1255852"
FT   CHAIN           2..152
FT                   /note="External scaffolding protein D"
FT                   /id="PRO_0000164880"
FT   MUTAGEN         61
FT                   /note="G->D: Confers a lethal phenotype."
FT                   /evidence="ECO:0000269|PubMed:12788631"
FT   MUTAGEN         61
FT                   /note="G->E: Confers a lethal phenotype."
FT                   /evidence="ECO:0000269|PubMed:12788631"
FT   MUTAGEN         61
FT                   /note="G->V: Confers a lethal phenotype."
FT                   /evidence="ECO:0000269|PubMed:12788631"
FT   HELIX           5..23
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           31..38
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:1CD3"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:1AL0"
FT   HELIX           48..59
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           61..65
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           75..85
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           88..97
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           104..109
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           117..129
FT                   /evidence="ECO:0007829|PDB:1TX9"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:1AL0"
SQ   SEQUENCE   152 AA;  16937 MW;  E8C912DCBA48D5E4 CRC64;
     MSQVTEQSVR FQTALASIKL IQASAVLDLT EDDFDFLTSN KVWIATDRSR ARRCVEACVY
     GTLDFVGYPR FPAPVEFIAA VIAYYVHPVN IQTACLIMEG AEFTENIING VERPVKAAEL
     FAFTLRVRAG NTDVLTDAEE NVRQKLRAEG VM