ID   VGA_BPPHK               Reviewed;         494 AA.
AC   P25244;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=A protein;
DE   AltName: Full=GPA;
GN   Name=A;
OS   Enterobacteria phage phiK (Bacteriophage phi-K).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Alphatrevirus.
OX   NCBI_TaxID=10848;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PHI-K AND MUTANT PHI KHT).
RX   PubMed=8827438; DOI=10.1093/oxfordjournals.jbchem.a021348;
RA   Kodaira K., Oki M., Kakikawa M., Kimoto H., Taketo A.;
RT   "The virion proteins encoded by bacteriophage phi K and its host-range
RT   mutant phi KhT: host-range determination and DNA binding properties.";
RL   J. Biochem. 119:1062-1069(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-257.
RX   PubMed=2785817; DOI=10.1016/0167-4781(89)90180-2;
RA   Kodaira K., Miyata T., Suzuki K., Nakano K., Taketo A.;
RT   "Possible finger structure in gene A protein of Microviridae.";
RL   Biochim. Biophys. Acta 1008:123-124(1989).
CC   -!- FUNCTION: The A protein is a specific endonuclease that cleaves the
CC       viral strand of supertwisted, closed circular DNA at a unique site in
CC       the A gene. The A protein also causes relaxation of supertwisted DNA
CC       and forms a complex with viral DNA that has a discontinuity in gene A
CC       of the viral strand.
CC   -!- MISCELLANEOUS: Phi KhT, a host-range mutant of phi K, can grow on
CC       E.coli C and B, besides K12, and is more thermosensitive than the
CC       parental phage phi K.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X60323; CAA42884.1; -; Genomic_DNA.
DR   EMBL; X12610; CAA31129.1; -; Genomic_DNA.
DR   PIR; S13753; S13753.
DR   RefSeq; NP_043942.1; NC_001730.1.
DR   GeneID; 1261192; -.
DR   KEGG; vg:1261192; -.
DR   Proteomes; UP000002122; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   InterPro; IPR008766; Replication_gene_A.
DR   Pfam; PF05840; Phage_GPA; 1.
PE   4: Predicted;
KW   DNA replication; DNA-binding; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Viral DNA replication; Zinc; Zinc-finger.
FT   CHAIN           1..494
FT                   /note="A protein"
FT                   /id="PRO_0000164866"
FT   ZN_FING         230..252
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        327
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        331
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  57285 MW;  7C8C6FB400090E13 CRC64;
     MATEIFSDVV KSVWSHATAK HAHLRMAVQV DNRSRLLSDL VYQLEKRLSE ETHLDDETYA
     LYESQTGLLE DHMALVRKCA AQLDNSNTID HRTPLDPECV FLFEMICPGV RYGKTLNSLW
     SKYAAQWPEK LIRQELDMVK PLSFKDEVAK YMEKMQEKTR KNRMTQKVIN EMRIAHQKGW
     FFVFDTLTLA DDRLQAFNEN PNALRDYFRT VGRAVLRAEG RSVKDSYNDC YRYLCVPEFG
     GQHGRLHWHV VHMVRTLPLG SHDPNFGRPV RNYRQINSFR GMWPYGFTQP IAVRYQHDAY
     SRKGWLWPVD KSGKAMQSKP YQAVAWYVTK YVAKQSDQRQ KAITERQKKC KNPLMAICLK
     KEFRVRSSRK LGMELPSMAH LSNKVLLELS RISFDSSPLY QIVKENAKKQ LTLNIGALPL
     HVILDVRPEV RSMLKAIRRL MKKTPEFNWQ SSIASMTVTL KNGDISDEAR QYIIDAGITP
     TDLRAKATQT FGGK