GP167_BPPZA
ID GP167_BPPZA Reviewed; 130 AA.
AC P08386;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 23-FEB-2022, entry version 71.
DE RecName: Full=DNA replication protein 16.7;
DE AltName: Full=Gene product 16.7;
DE Short=gp16.7;
DE AltName: Full=Protein p16.7;
GN Name=16.7;
OS Bacillus phage PZA (Bacteriophage PZA).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus; Bacillus virus PZA.
OX NCBI_TaxID=10757;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3095189; DOI=10.1016/0378-1119(86)90049-1;
RA Paces V., Vlcek C., Urbanek P., Hostomsky Z.;
RT "Nucleotide sequence of the right early region of Bacillus subtilis phage
RT PZA completes the 19366-bp sequence of PZA genome. Comparison with the
RT homologous sequence of phage phi 29.";
RL Gene 44:115-120(1986).
CC -!- FUNCTION: Binds to the long stretches of ssDNA of the viral DNA
CC replication intermediates created during the protein-primed mechanism
CC of replication of the viral genome and attaches the viral DNA to the
CC membrane of the infected cells. Required for the redistribution of
CC replicating viral DNA from the initial replication site to membrane-
CC associated sites surrounding the nucleoid. Required for the second pull
CC step of DNA ejection. {ECO:0000250|UniProtKB:P16517}.
CC -!- SUBUNIT: Homodimer; homooligomer. Interacts with DNA; one dsDNA binding
CC subunit is constituted by three p16.7 dimers.
CC {ECO:0000250|UniProtKB:P16517}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane
CC {ECO:0000250|UniProtKB:P16517}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P16517}.
CC -!- SIMILARITY: Belongs to the phi29likevirus gp16.7 family. {ECO:0000305}.
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DR EMBL; M11813; AAA88496.1; -; Genomic_DNA.
DR PIR; C29004; WRBP67.
DR SMR; P08386; -.
DR TCDB; 9.B.80.1.1; the bacillus phage Phi29 (a podovirus) dna ejection system (Phi29-e) family.
DR Proteomes; UP000000855; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.600; -; 1.
DR InterPro; IPR009595; Phage_DNA_replic_GP16.7.
DR InterPro; IPR037211; Phage_DNA_replic_GP16.7_sf.
DR Pfam; PF06720; Phi-29_GP16_7; 1.
DR SUPFAM; SSF140713; SSF140713; 1.
PE 3: Inferred from homology;
KW Coiled coil; DNA replication; DNA-binding; Early protein;
KW Host cell membrane; Host membrane; Membrane; Transmembrane;
KW Transmembrane helix; Viral DNA replication.
FT CHAIN 1..130
FT /note="DNA replication protein 16.7"
FT /id="PRO_0000106615"
FT TRANSMEM 1..20
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P16517"
FT REGION 70..130
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P16517"
FT COILED 18..57
FT /evidence="ECO:0000255"
FT SITE 113
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250|UniProtKB:P16517"
FT SITE 116
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250|UniProtKB:P16517"
FT SITE 120
FT /note="Involved in oligomerization and DNA binding"
FT /evidence="ECO:0000250|UniProtKB:P16517"
SQ SEQUENCE 130 AA; 15222 MW; CC078208C152C4A3 CRC64;
MEAILMIGVI TLCVIFLLSG RNNKKIQEAR ELEDYLEDLN QRIAQRTQIL SELNEVITNR
SVDKSVNMSA CEIAVLDLYE QSNIRIPSDI IEDMVNQRLQ TEQDVLNYIE TQRTYWKLEN
QKKLYRGSLK