ID   GP12_BPT7               Reviewed;          85 AA.
AC   P03780;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Inhibitor of dGTPase;
DE   AltName: Full=Gene product 1.2;
DE            Short=Gp1.2;
DE   AltName: Full=Inhibitor of dGTPase gp1.2;
GN   OrderedLocusNames=1.2;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA   Dunn J.J., Studier F.W.;
RT   "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT   the beginning of gene 4.";
RL   J. Mol. Biol. 148:303-330(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6254001; DOI=10.1073/pnas.77.7.3917;
RA   Saito H., Tabor S., Tamanoi F., Richardson C.C.;
RT   "Nucleotide sequence of the primary origin of bacteriophage T7 DNA
RT   replication: relationship to adjacent genes and regulatory elements.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:3917-3921(1980).
RN   [4]
RP   FUNCTION.
RX   PubMed=3549718; DOI=10.1016/s0021-9258(18)61186-x;
RA   Myers J.A., Beauchamp B.B., Richardson C.C.;
RT   "Gene 1.2 protein of bacteriophage T7. Effect on deoxyribonucleotide
RT   pools.";
RL   J. Biol. Chem. 262:5288-5292(1987).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH HOST DGT.
RX   PubMed=2155228; DOI=10.1016/s0021-9258(19)39580-8;
RA   Nakai H., Richardson C.C.;
RT   "The gene 1.2 protein of bacteriophage T7 interacts with the Escherichia
RT   coli dGTP triphosphohydrolase to form a GTP-binding protein.";
RL   J. Biol. Chem. 265:4411-4419(1990).
CC   -!- FUNCTION: Plays a role in increasing the intracellular pool of dGTP.
CC       Interacts with and inhibits host dGTPase/dgt. The complex made of the
CC       host dGTPase and gene 1.2 protein creates a GTP-binding site of high
CC       affinity. Subsequent binding of GTP to the enzyme-inhibitor complex
CC       inhibits its dissociation. {ECO:0000269|PubMed:2155228,
CC       ECO:0000269|PubMed:3549718}.
CC   -!- SUBUNIT: Interacts with host dGTPase/dgt. {ECO:0000269|PubMed:2155228}.
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DR   EMBL; V01146; CAA24392.1; -; Genomic_DNA.
DR   EMBL; V01126; CAA24325.1; -; Genomic_DNA.
DR   EMBL; V01127; CAA24335.1; -; Genomic_DNA.
DR   PIR; F43002; W1BP27.
DR   RefSeq; NP_041962.1; NC_001604.1.
DR   PDB; 2MDP; NMR; -; A=1-85.
DR   PDBsum; 2MDP; -.
DR   BMRB; P03780; -.
DR   SMR; P03780; -.
DR   GeneID; 1261049; -.
DR   KEGG; vg:1261049; -.
DR   Proteomes; UP000000840; Genome.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR020147; Phage_T7-like_1.2.
DR   Pfam; PF10922; DUF2745; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; Early protein; Host-virus interaction;
KW   Reference proteome.
FT   CHAIN           1..85
FT                   /note="Inhibitor of dGTPase"
FT                   /id="PRO_0000106470"
FT   HELIX           9..21
FT                   /evidence="ECO:0007829|PDB:2MDP"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:2MDP"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:2MDP"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:2MDP"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:2MDP"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:2MDP"
FT   HELIX           63..83
FT                   /evidence="ECO:0007829|PDB:2MDP"
SQ   SEQUENCE   85 AA;  10190 MW;  EE292B9102BE2650 CRC64;
     MGRLYSGNLA AFKAATNKLF QLDLAVIYDD WYDAYTRKDC IRLRIEDRSG NLIDTSTFYH
     HDEDVLFNMC TDWLNHMYDQ LKDWK