ID   REP_BPM13               Reviewed;         410 AA.
AC   P69547; P03659;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 61.
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 M13 (Bacteriophage M13).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Inovirus.
OX   NCBI_TaxID=1977402;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6254849; DOI=10.1016/0378-1119(80)90093-1;
RA   van Wezenbeek P.M.G.F., Hulsebos T.J.M., Schoenmakers J.G.G.;
RT   "Nucleotide sequence of the filamentous bacteriophage M13 DNA genome:
RT   comparison with phage fd.";
RL   Gene 11:129-148(1980).
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=P69547-1; Sequence=Displayed;
CC       Name=G10P; Synonyms=Gene 10 protein;
CC         IsoId=P69547-2; Sequence=VSP_018671;
CC   -!- MISCELLANEOUS: [Isoform G10P]: N-formylation on Met-300. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the inovirus G2P protein family. {ECO:0000305}.
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DR   EMBL; V00604; CAA23856.1; -; Genomic_DNA.
DR   EMBL; V00604; CAA23857.1; -; Genomic_DNA.
DR   PIR; B04264; Z2BPM3.
DR   Proteomes; UP000002111; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Alternative initiation; ATP-binding; DNA replication; DNA-binding;
KW   Endonuclease; Formylation; Hydrolase; Ligase; Nuclease; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..410
FT                   /note="Replication-associated protein G2P"
FT                   /id="PRO_0000003307"
FT   VAR_SEQ         1..299
FT                   /note="Missing (in isoform G10P)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018671"
SQ   SEQUENCE   410 AA;  46167 MW;  810385EF8B43AFEA 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
     LVRFEARIKT RYLKSFGLPL NLFDAIRFAS DYNSQGKDLI FDLWSFSFSE LFKAFEGDSM
     NIYDDSAVLD AIQSKHFTIT PSGKTSFAKA SRYFGFYRRL VNEGYDSVAL TMPRNSFWRY
     VSALVECGIP KSQLMNLSTC NNVVPLVRFI NVDFSSQRPD WYNEPVLKIA