ID   REP_BPIKE               Reviewed;         421 AA.
AC   P03660;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Salmonella phage IKe (Bacteriophage IKe).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Lineavirus.
OX   NCBI_TaxID=10867;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3981635; DOI=10.1016/0022-2836(85)90322-5;
RA   Peeters B.P.H., Peters R.M., Schoenmakers J.G.G., Konings R.N.H.;
RT   "Nucleotide sequence and genetic organization of the genome of the N-
RT   specific filamentous bacteriophage IKe. Comparison with the genome of the
RT   F-specific filamentous phages M13, fd and f1.";
RL   J. Mol. Biol. 181:27-39(1985).
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=P03660-1; Sequence=Displayed;
CC       Name=G10P; Synonyms=Gene 10 protein;
CC         IsoId=P03660-2; Sequence=VSP_018673;
CC   -!- SIMILARITY: Belongs to the inovirus G2P protein family. {ECO:0000305}.
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DR   EMBL; X02139; CAA26067.1; -; Genomic_DNA.
DR   EMBL; X02139; CAA26068.1; -; Genomic_DNA.
DR   PIR; A04265; Z2BPIK.
DR   RefSeq; NP_040570.1; NC_002014.1. [P03660-1]
DR   RefSeq; NP_040571.1; NC_002014.1. [P03660-2]
DR   GeneID; 1260890; -.
DR   GeneID; 1260892; -.
DR   KEGG; vg:1260890; -.
DR   KEGG; vg:1260892; -.
DR   Proteomes; UP000000372; 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   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   3: Inferred from homology;
KW   Alternative initiation; DNA replication; DNA-binding; Endonuclease;
KW   Hydrolase; Ligase; Nuclease; Reference proteome.
FT   CHAIN           1..421
FT                   /note="Replication-associated protein G2P"
FT                   /id="PRO_0000003311"
FT   VAR_SEQ         1..300
FT                   /note="Missing (in isoform G10P)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018673"
SQ   SEQUENCE   421 AA;  47594 MW;  626AC1FDDF4E5215 CRC64;
     MIDMLVLRIP FKSSLVSERL DSKGNYVSHV NLAEVARLSG LTLAAHTVEY AIDGDLTVSG
     LKHPYESLPS HYAGIALKIF EGGKNFEPCV ELKASPAKLL QGHNVFGPTS FELCGLEFFG
     AFAAAMPELY DLCDVTNTVV GRIDVTFSAK VANDHIANQV ISFLRNVSNG QTKKTRALDY
     ETTVMWNEGS RHRTLVAYLK HHEVQAQIKR LQKKKSSHLT IYEKNCLEVL SNPDLQLYAV
     GLVRFEARLH TRFFENFGLP RKFFDIVKYQ DNYESGSFNL ICDLWKKSFK DLFDAFKGSD
     MNVYDDSKVY DALINNFSSV TKSGNISNSK ANRLFGFYRR LVNEGYDNVA QTMERTTFWR
     SLKELTSVGL SKAQLMNLST DNNVVPLVQM INVDFSQQYP EWYVEPVSIF NRSNVVSINA
     A