SCAF_BPPH2
ID SCAF_BPPH2 Reviewed; 98 AA.
AC P13848; B3VMP2; Q70AA8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Capsid assembly scaffolding protein {ECO:0000303|PubMed:17198713};
DE AltName: Full=Gene product 7 {ECO:0000305};
DE Short=gp7 {ECO:0000305};
DE AltName: Full=Head morphogenesis protein {ECO:0000305};
DE AltName: Full=Protein p7 {ECO:0000305};
DE AltName: Full=Scaffold protein {ECO:0000305};
GN Name=7;
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3763399; DOI=10.1093/nar/14.17.7129;
RA Innis C.A., Garvey K.J., Ito J.;
RT "Nucleotide sequence of phage phi 29 gene 7: structure of intergenic spacer
RT between the major early and late genes.";
RL Nucleic Acids Res. 14:7129-7129(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-65.
RC STRAIN=PhiFZB24 {ECO:0000312|EMBL:CAE54613.1};
RX PubMed=11381102; DOI=10.1128/mmbr.65.2.261-287.2001;
RA Meijer W.J.J., Horcajadas J.A., Salas M.;
RT "Phi29 family of phages.";
RL Microbiol. Mol. Biol. Rev. 65:261-287(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-65.
RC STRAIN=PhiFZB24 {ECO:0000312|EMBL:CAE54613.1};
RA Borriss R., Diesner M.O., Maennel A., Gelderblom H.;
RT "Morphological and molecular characterization of a Bacillus phage isolated
RT from a fermentation plant.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11562162; DOI=10.1006/jsbi.2001.4375;
RA Peterson C., Simon M., Hodges J., Mertens P., Higgins L., Egelman E.,
RA Anderson D.;
RT "Composition and mass of the bacteriophage phi29 prohead and virion.";
RL J. Struct. Biol. 135:18-25(2001).
RN [7]
RP FUNCTION.
RX PubMed=17098197; DOI=10.1016/j.str.2006.09.007;
RA Choi K.H., Morais M.C., Anderson D.L., Rossmann M.G.;
RT "Determinants of bacteriophage phi29 head morphology.";
RL Structure 14:1723-1727(2006).
RN [8]
RP FUNCTION.
RX PubMed=17198713; DOI=10.1016/j.jmb.2006.11.091;
RA Fu C.Y., Morais M.C., Battisti A.J., Rossmann M.G., Prevelige P.E. Jr.;
RT "Molecular dissection of phi29 scaffolding protein function in an in vitro
RT assembly system.";
RL J. Mol. Biol. 366:1161-1173(2007).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLU-56 AND ARG-69.
RX PubMed=23896641; DOI=10.1016/j.virol.2013.07.001;
RA Li R., Cherwa J.E. Jr., Prevelige P.E. Jr.;
RT "Phi29 scaffolding and connector structure-function relationship studied by
RT trans-complementation.";
RL Virology 444:355-362(2013).
RN [10] {ECO:0007744|PDB:1NO4, ECO:0007744|PDB:1NOH}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-98, DNA-BINDING, FUNCTION, AND
RP SUBUNIT.
RX PubMed=12778115; DOI=10.1038/nsb939;
RA Morais M.C., Kanamaru S., Badasso M.O., Koti J.S., Owen B.A.,
RA McMurray C.T., Anderson D.L., Rossmann M.G.;
RT "Bacteriophage phi29 scaffolding protein gp7 before and after prohead
RT assembly.";
RL Nat. Struct. Biol. 10:572-576(2003).
CC -!- FUNCTION: Scaffolding protein involved in the icosahedric procapsid
CC assembly. Coassembles with the capsid proteins to form the procapsid.
CC The scaffolding protein is found within the capsid as a serie of
CC concentric shells. During DNA packaging, the scaffolding protein
CC molecules are released from the procapsid.
CC {ECO:0000269|PubMed:12778115, ECO:0000269|PubMed:17098197,
CC ECO:0000305|PubMed:17198713, ECO:0000305|PubMed:23896641}.
CC -!- SUBUNIT: Homodimer. Interacts non-specifically with DNA; probably binds
CC DNA in the early stages of DNA packaging.
CC {ECO:0000269|PubMed:12778115}.
CC -!- SUBCELLULAR LOCATION: Note=Present in about 147 copies in the prohead
CC but not present in mature virions. {ECO:0000269|PubMed:11562162}.
CC -!- SIMILARITY: Belongs to the phi29likevirus scaffolding protein family.
CC {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; M14782; AAA32279.1; -; Genomic_DNA.
DR EMBL; X04386; CAA27974.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96029.1; -; Genomic_DNA.
DR EMBL; AJ606486; CAE54613.1; -; Genomic_DNA.
DR PIR; A28923; WMBPF9.
DR RefSeq; YP_002004535.1; NC_011048.1.
DR PDB; 1NO4; X-ray; 2.20 A; A/B/C/D=2-98.
DR PDB; 1NOH; X-ray; 2.80 A; A/B/C/D=2-98.
DR PDB; 3MTU; X-ray; 2.10 A; E/F=2-46.
DR PDB; 3OA7; X-ray; 2.30 A; A=2-50.
DR PDB; 4IFF; X-ray; 2.30 A; A/B/C/D=2-48.
DR PDB; 4XA1; X-ray; 3.20 A; A/B/C/D=1-49.
DR PDB; 4XA3; X-ray; 2.55 A; A/B=1-49.
DR PDB; 4XA6; X-ray; 3.42 A; A/B/C/D=2-50.
DR PDB; 5CJ1; X-ray; 2.10 A; A/B/C/D/E/F/G/H=2-52.
DR PDB; 5WJB; X-ray; 2.90 A; A/B/C/D=2-48.
DR PDB; 5WLQ; X-ray; 3.10 A; A=2-48.
DR PDB; 5WME; X-ray; 2.30 A; A/B/C/D=2-52.
DR PDB; 6PFP; X-ray; 2.20 A; A/B/C/D=2-48.
DR PDB; 6YJD; X-ray; 2.90 A; A=1-54.
DR PDBsum; 1NO4; -.
DR PDBsum; 1NOH; -.
DR PDBsum; 3MTU; -.
DR PDBsum; 3OA7; -.
DR PDBsum; 4IFF; -.
DR PDBsum; 4XA1; -.
DR PDBsum; 4XA3; -.
DR PDBsum; 4XA6; -.
DR PDBsum; 5CJ1; -.
DR PDBsum; 5WJB; -.
DR PDBsum; 5WLQ; -.
DR PDBsum; 5WME; -.
DR PDBsum; 6PFP; -.
DR PDBsum; 6YJD; -.
DR SMR; P13848; -.
DR GeneID; 6446525; -.
DR KEGG; vg:6446525; -.
DR EvolutionaryTrace; P13848; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0046806; C:viral scaffold; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR038032; Gp7.
DR InterPro; IPR024374; Phage_phi-29_Gp7.
DR Pfam; PF11418; Scaffolding_pro; 1.
DR SUPFAM; SSF90246; SSF90246; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA-binding; Late protein; Reference proteome;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..98
FT /note="Capsid assembly scaffolding protein"
FT /id="PRO_0000106571"
FT COILED 40..62
FT /evidence="ECO:0000255"
FT MUTAGEN 56
FT /note="E->K: Forms procapsids which have incorporated the
FT connector. Defective in producing infectious virions."
FT /evidence="ECO:0000269|PubMed:23896641"
FT MUTAGEN 69
FT /note="R->E: Fails to incorporate the connector. Defective
FT in producing infectious virions."
FT /evidence="ECO:0000269|PubMed:23896641"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:3MTU"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:6YJD"
FT HELIX 23..46
FT /evidence="ECO:0007829|PDB:3MTU"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:3MTU"
SQ SEQUENCE 98 AA; 11267 MW; FF2E7985D2266E14 CRC64;
MPLKPEEHED ILNKLLDPEL AQSERTEALQ QLRVNYGSFV SEYNDLTKSH EKLAAEKDDL
IVSNSKLFRQ IGLTDKQEED HKKADISETI TIEDLEAK
