ID   REP_BPPHM               Reviewed;         315 AA.
AC   Q9G050;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Replication-associated protein VP4;
DE            Short=Rep;
DE            Short=VP4;
DE            EC=3.1.21.-;
DE            EC=6.5.1.1;
GN   ORFNames=ORF4;
OS   Bdellovibrio phage phiMH2K (Bacteriophage phiMH2K).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Gokushovirinae; Bdellomicrovirus.
OX   NCBI_TaxID=145579;
OH   NCBI_TaxID=959; Bdellovibrio bacteriovorus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11807069; DOI=10.1128/jb.184.4.1089-1094.2002;
RA   Brentlinger K.L., Hafenstein S., Novak C.R., Fane B.A., Borgon R.,
RA   McKenna R., Agbandje-McKenna M.;
RT   "Microviridae, a family divided: isolation, characterization, and genome
RT   sequence of phiMH2K, a bacteriophage of the obligate intracellular
RT   parasitic bacterium Bdellovibrio bacteriovorus.";
RL   J. Bacteriol. 184:1089-1094(2002).
CC   -!- FUNCTION: Plays an essential role in viral DNA replication. Binds the
CC       origin of replication and cleaves the dsDNA replicative form I (RFI)
CC       and becomes covalently bound to it via phosphotyrosine bond, generating
CC       the dsDNA replicative form II (RFII). In turn, viral DNA replication
CC       initiates at the 3'-OH of the cleavage site. After one round of rolling
CC       circle synthesis, protein VP4 is linked to the newly synthesized ssDNA
CC       and joins the ends of the displaced strand to generate a circular
CC       single-stranded molecule ready to be packed into a virion.
CC       {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   -!- SIMILARITY: Belongs to the microviridae Rep protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF306496; AAG45349.1; -; Genomic_DNA.
DR   RefSeq; NP_073537.1; NC_002643.1.
DR   GeneID; 918747; -.
DR   KEGG; vg:918747; -.
DR   Proteomes; UP000002418; Genome.
DR   GO; GO:0005524; F:ATP 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.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Endonuclease; Hydrolase; Ligase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..315
FT                   /note="Replication-associated protein VP4"
FT                   /id="PRO_0000372064"
FT   COILED          253..315
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        176
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  37232 MW;  EB0BC61D3CF67BFB CRC64;
     MHCIRPIKAG FNATGDIVYS SKKISKELAS FAFPCRKCIP CRLNMAREKA IRAYHESQMW
     DDNIFLTLTY DDEHLKSDRL QWIDFDLFIK RLNEKLNRGL SKENRRPLPY MVTGEYGDKT
     KRPHWHVLIF NFRPDDAKKH YVTELGEQVY TSEFIRDLWT HGNIEFGSVT LDSASYVARY
     AAKKLAHGND QDHDYHPIHN TSKKHAIGKK WIEKYHEQTF SRGYVVLPNG SQGPIPRYYQ
     DWYKKNHPEK WMEYDAKVKL KSKELAEMQS RKDQLDDFAN FINYRGGTNY PLSRTQVKLA
     ILKSKFKQLQ EKLKL