GP1_BPPH2
ID GP1_BPPH2 Reviewed; 86 AA.
AC P03679; Q6LDQ0; Q6LDQ1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 29-SEP-2021, entry version 80.
DE RecName: Full=DNA replication protein 1 {ECO:0000303|PubMed:9774353};
DE AltName: Full=Gene product 1 {ECO:0000305};
DE Short=gp1 {ECO:0000305};
GN Name=1;
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] (ISOFORMS LONG AND SHORT), AND PROTEIN
RP SEQUENCE OF 2-9 AND 35-41.
RX PubMed=2526779; DOI=10.1016/0378-1119(89)90067-x;
RA Prieto I., Mendez E., Salas M.;
RT "Characterization, overproduction and purification of the product of gene 1
RT of Bacillus subtilis phage phi 29.";
RL Gene 77:195-204(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
RX PubMed=6809534; DOI=10.1016/0378-1119(82)90149-4;
RA Yoshikawa H., Ito J.;
RT "Nucleotide sequence of the major early region of bacteriophage phi 29.";
RL Gene 17:323-335(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
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 FUNCTION.
RX PubMed=9193003; DOI=10.1006/jmbi.1997.1032;
RA Bravo A., Salas M.;
RT "Initiation of bacteriophage phi29 DNA replication in vivo: assembly of a
RT membrane-associated multiprotein complex.";
RL J. Mol. Biol. 269:102-112(1997).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9774353; DOI=10.1093/emboj/17.20.6096;
RA Bravo A., Salas M.;
RT "Polymerization of bacteriophage phi 29 replication protein p1 into
RT protofilament sheets.";
RL EMBO J. 17:6096-6105(1998).
RN [6]
RP RNA-BINDING.
RX PubMed=9480849; DOI=10.1006/bbrc.1998.8139;
RA Takeuchi A., Makino O., Hirokawa H.;
RT "Gene 1, one of the dna genes of bacteriophage phi 29, represses other dna
RT genes through binding to mRNA.";
RL Biochem. Biophys. Res. Commun. 243:566-571(1998).
RN [7]
RP DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH THE PRIMER TERMINAL PROTEIN,
RP AND FUNCTION.
RX PubMed=11032825; DOI=10.1093/emboj/19.20.5575;
RA Bravo A., Illana B., Salas M.;
RT "Compartmentalization of phage phi29 DNA replication: interaction between
RT the primer terminal protein and the membrane-associated protein p1.";
RL EMBO J. 19:5575-5584(2000).
RN [8]
RP COILED COIL, AND MUTAGENESIS OF LEU-40; LEU-47; MET-54 AND LEU-61.
RX PubMed=11283004; DOI=10.1074/jbc.m011296200;
RA Bravo A., Serrano-Heras G., Salas M.;
RT "A single amino acid substitution within a coiled-coil motif changes the
RT assembly of a 53-amino acid protein from two-dimensional sheets to
RT filamentous structures.";
RL J. Biol. Chem. 276:21250-21256(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12904294; DOI=10.1074/jbc.m306935200;
RA Serrano-Heras G., Salas M., Bravo A.;
RT "In vivo assembly of phage phi 29 replication protein p1 into membrane-
RT associated multimeric structures.";
RL J. Biol. Chem. 278:40771-40777(2003).
RN [10]
RP RNA-BINDING, SUBUNIT, AND MUTAGENESIS OF LYS-3; LYS-9; LYS-34; LYS-42;
RP TRP-72; LYS-75 AND PHE-78.
RX PubMed=15883018; DOI=10.1016/j.bbrc.2005.04.056;
RA Hashiyama K., Takeuchi A., Makino O.;
RT "Effects of single amino acid substitutions at the predicted coiled-coil or
RT hydrophobic region on the self-assembly of phi29 replication protein,
RT gp1.";
RL Biochem. Biophys. Res. Commun. 331:1310-1316(2005).
RN [11]
RP INTERACTION WITH BACILLUS SUBTILIS FTSZ.
RX PubMed=23836667; DOI=10.1073/pnas.1311524110;
RA Ballesteros-Plaza D., Holguera I., Scheffers D.J., Salas M.,
RA Munoz-Espin D.;
RT "Phage 29 phi protein p1 promotes replication by associating with the FtsZ
RT ring of the divisome in Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:12313-12318(2013).
CC -!- FUNCTION: Protein that assembles into highly ordered structures and
CC provides a specific site for viral DNA replication. Probably anchors
CC the viral DNA replisome to the host membrane.
CC {ECO:0000269|PubMed:11032825, ECO:0000269|PubMed:12904294,
CC ECO:0000269|PubMed:9193003, ECO:0000269|PubMed:9774353}.
CC -!- SUBUNIT: Homomultimer. Self-associates into large complexes forming
CC long filamentous structures (PubMed:2526779) (PubMed:9774353,
CC PubMed:15883018). Interacts (via N-terminus) with the primer terminal
CC protein (PubMed:11032825). Interacts with host FtsZ protein
CC (PubMed:23836667). {ECO:0000269|PubMed:15883018,
CC ECO:0000269|PubMed:23836667, ECO:0000269|PubMed:2526779,
CC ECO:0000269|PubMed:9774353}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000269|PubMed:11032825,
CC ECO:0000269|PubMed:12904294}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12904294}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long; Synonyms=10 kDa;
CC IsoId=P03679-1; Sequence=Displayed;
CC Name=Short; Synonyms=6 kDa, Protein delta-1;
CC IsoId=P03679-2; Sequence=VSP_018684;
CC -!- DOMAIN: The hydrophobic C-terminus is involved in the association with
CC the host membrane (PubMed:11032825). The coiled coil region is involved
CC assembly into protofilament sheet structures (PubMed:11283004).
CC {ECO:0000269|PubMed:11032825, ECO:0000269|PubMed:11283004}.
CC -!- SIMILARITY: Belongs to the phi29likevirus DNA replication protein 1
CC family. {ECO:0000305}.
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DR EMBL; M26968; AAB59294.1; -; Genomic_DNA.
DR EMBL; M26968; AAB59295.1; -; Genomic_DNA.
DR EMBL; V01155; CAA24478.1; -; Genomic_DNA.
DR EMBL; V01155; CAA24479.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96022.1; -; Genomic_DNA.
DR PIR; A04281; ERBP19.
DR RefSeq; YP_002004528.1; NC_011048.1. [P03679-1]
DR SMR; P03679; -.
DR GeneID; 6446501; -.
DR KEGG; vg:6446501; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0033644; C:host cell membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR InterPro; IPR016408; Phage_phi-29_Gp1.
DR PIRSF; PIRSF004177; gp1_phi29; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Coiled coil; Direct protein sequencing;
KW DNA replication; Early protein; Host membrane; Membrane;
KW Reference proteome; RNA-binding; Viral DNA replication.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2526779"
FT CHAIN 2..86
FT /note="DNA replication protein 1"
FT /id="PRO_0000003359"
FT COILED 38..67
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018684"
FT MUTAGEN 3
FT /note="K->E: No effect on self-assembly."
FT /evidence="ECO:0000269|PubMed:15883018"
FT MUTAGEN 9
FT /note="K->E: No effect on self-assembly."
FT /evidence="ECO:0000269|PubMed:15883018"
FT MUTAGEN 34
FT /note="K->E: Unable to form multimers larger than
FT tetramers."
FT /evidence="ECO:0000269|PubMed:15883018"
FT MUTAGEN 40
FT /note="L->A: Assembles as protofilament sheets like the
FT wild type."
FT /evidence="ECO:0000269|PubMed:11283004"
FT MUTAGEN 42
FT /note="K->E: Unable to form multimers larger than
FT tetramers."
FT /evidence="ECO:0000269|PubMed:15883018"
FT MUTAGEN 47
FT /note="L->V: Assembles as 10-nm filamentous structures."
FT /evidence="ECO:0000269|PubMed:11283004"
FT MUTAGEN 54
FT /note="M->A: Cannot assemble as highly ordered structures."
FT /evidence="ECO:0000269|PubMed:11283004"
FT MUTAGEN 61
FT /note="L->I: Assembles as small oligomeric structures which
FT cannot assemble further into larger arrays."
FT /evidence="ECO:0000269|PubMed:11283004"
FT MUTAGEN 72
FT /note="W->R: Unable to form multimers larger than
FT tetramers."
FT /evidence="ECO:0000269|PubMed:15883018"
FT MUTAGEN 75
FT /note="K->E: Unable to form multimers larger than
FT tetramers."
FT /evidence="ECO:0000269|PubMed:15883018"
FT MUTAGEN 78
FT /note="F->S: Unable to form multimers larger than
FT tetramers."
FT /evidence="ECO:0000269|PubMed:15883018"
SQ SEQUENCE 86 AA; 9892 MW; 3EF441D477BDE7CE CRC64;
MGKIFDQEKR LEGTWKNSKW GNQGIIAPVD GDLKMIDLEL EKKMTKLEHE NKLMKNALYE
LSRMENNDYA TWVIKVLFGG APHGAK
