ID   REP_BPF1                Reviewed;         410 AA.
AC   P69546; P03659;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Replication-associated protein G2P;
DE            Short=Rep;
DE            EC=3.1.21.-;
DE            EC=6.5.1.1;
DE   AltName: Full=G2P;
DE   AltName: Full=Gene 2 protein;
GN   Name=II;
OS   Enterobacteria phage f1 (Bacteriophage f1).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Inovirus.
OX   NCBI_TaxID=10863;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6282703; DOI=10.1016/0378-1119(81)90059-7;
RA   Beck E., Zink B.;
RT   "Nucleotide sequence and genome organisation of filamentous bacteriophages
RT   f1 and fd.";
RL   Gene 16:35-58(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6292494; DOI=10.1128/jvi.44.1.32-46.1982;
RA   Hill D.F., Petersen G.B.;
RT   "Nucleotide sequence of bacteriophage f1 DNA.";
RL   J. Virol. 44:32-46(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX   PubMed=439137; DOI=10.1016/0022-2836(79)90090-1;
RA   Ravetch J.V., Horiuchi K., Zinder N.D.;
RT   "DNA sequence analysis of the defective interfering particles of
RT   bacteriophage f1.";
RL   J. Mol. Biol. 128:305-318(1979).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-132.
RX   PubMed=353810; DOI=10.1073/pnas.75.5.2266;
RA   Ravetch J.V., Horiuchi K., Zinder N.D.;
RT   "Nucleotide sequence of the recognition site for the restriction-
RT   modification enzyme of Escherichia coli B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:2266-2270(1978).
RN   [5]
RP   IDENTIFICATION OF PROTEIN, AND FORMYLATION AT MET-1 (ISOFORM G10P).
RX   PubMed=7026565; DOI=10.1016/s0021-9258(19)68586-8;
RA   Yen T.S.B., Webster R.E.;
RT   "Bacteriophage f1 gene II and X proteins. Isolation and characterization of
RT   the products of two overlapping genes.";
RL   J. Biol. Chem. 256:11259-11265(1981).
CC   -!- FUNCTION: Isoform G2P plays an essential role in viral DNA replication.
CC       Binds the origin of replication and cleaves the dsDNA replicative form
CC       I (RFI) and becomes covalently bound to it via phosphotyrosine bond,
CC       generating the dsDNA replicative form II (RFII). In turn, viral DNA
CC       replication initiates at the 3'-OH of the cleavage site. After one
CC       round of rolling circle synthesis, protein G2P is linked to the newly
CC       synthesized ssDNA and joins the ends of the displaced strand to
CC       generate a circular single-stranded molecule ready to be packed into a
CC       virion. {ECO:0000250}.
CC   -!- FUNCTION: Isoform G10P protein binds to double-stranded DNA and
CC       prevents hydrolysis by nucleases. Additionally, G10P is an inhibitor of
CC       DNA replication and may have a role in the transition from
CC       semiconservative replicative form DNA replication to single-stranded
CC       DNA synthesis in the life cycle. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=G2P; Synonyms=Gene 2 protein;
CC         IsoId=P69546-1; Sequence=Displayed;
CC       Name=G10P; Synonyms=Gene 10 protein;
CC         IsoId=P69546-2; Sequence=VSP_018670;
CC   -!- SIMILARITY: Belongs to the inovirus G2P protein family. {ECO:0000305}.
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DR   EMBL; V00606; CAA23876.1; -; Genomic_DNA.
DR   EMBL; V00606; CAA23867.1; -; Genomic_DNA.
DR   EMBL; J02448; AAA32209.1; -; Genomic_DNA.
DR   EMBL; J02448; AAA32210.1; -; Genomic_DNA.
DR   EMBL; M10641; AAA32223.1; -; Genomic_DNA.
DR   EMBL; M10744; AAA32225.1; -; Genomic_DNA.
DR   PIR; C04264; Z2BPF1.
DR   Proteomes; UP000002557; Genome.
DR   Proteomes; UP000241027; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
DR   InterPro; IPR006516; G2P.
DR   InterPro; IPR022688; G2P_C.
DR   InterPro; IPR022686; G2P_N.
DR   Pfam; PF05144; Phage_CRI; 1.
DR   Pfam; PF05155; Phage_X; 1.
DR   TIGRFAMs; TIGR01629; rep_II_X; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; DNA replication; DNA-binding; Endonuclease;
KW   Formylation; Hydrolase; Ligase; Nuclease.
FT   CHAIN           1..410
FT                   /note="Replication-associated protein G2P"
FT                   /id="PRO_0000003305"
FT   VAR_SEQ         1..299
FT                   /note="Missing (in isoform G10P)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018670"
FT   MOD_RES         P69546-2:1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:7026565"
SQ   SEQUENCE   410 AA;  46168 MW;  6CB09CDBDFC98FE2 CRC64;
     MIDMLVLRLP FIDSLVCSRL SGNDLIAFVD LSKIATLSGM NLSARTVEYH IDGDLTVSGL
     SHPFESLPTH YSGIAFKIYE GSKNFYPCVE IKASPAKVLQ GHNVFGTTDL ALCSEALLLN
     FANSLPCLYD LLDVNATTIS RIDATFSARA PNENIAKQVI DHLRNVSNGQ TKSTRSQNWE
     STVTWNETSR HRTLVAYLKH VELQHQIQQL SSKPSAKMTS YQKEQLKVLS NPDLLEFASG
     LVRFEARIET RYLKSFGLPL NLFDAIRFAS DYNSQGKDLI FDLWSFSFSE LFKAFEGDSM
     NIYDDSAVLD AIQSKHFTIT PSGKTSFAKA SRYFGFYRRL VNEGYDSVAL TMPRNSFWRY
     VSALVECGIP KSQLMNLSTC NNVVPLVRFI NVDFSSQRPD WYNEPVLKIA