ID   G1P_BPFD                Reviewed;         348 AA.
AC   P03655;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Gene 1 protein;
DE   AltName: Full=G1P;
GN   Name=I;
OS   Enterobacteria phage fd (Bacteriophage fd).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Inovirus.
OX   NCBI_TaxID=2847073;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=478 / Heidelberg;
RX   PubMed=745987; DOI=10.1093/nar/5.12.4495;
RA   Beck E., Sommer R., Auerswald E.A., Kurz C., Zink B., Osterburg G.,
RA   Schaller H., Sugimoto K., Sugisaki H., Okamoto T., Takanami M.;
RT   "Nucleotide sequence of bacteriophage fd DNA.";
RL   Nucleic Acids Res. 5:4495-4503(1978).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2457024; DOI=10.1016/s0021-9258(18)37998-5;
RA   Horabin J.I., Webster R.E.;
RT   "An amino acid sequence which directs membrane insertion causes loss of
RT   membrane potential.";
RL   J. Biol. Chem. 263:11575-11583(1988).
CC   -!- FUNCTION: Isoform G1P plays an essential role in phage assembly. It is
CC       required to increase the number of adhesion zones between the inner and
CC       outer membranes of the host cell. The extrusion of neo-synthesized
CC       phages occurs at these adhesion sites. May be involved with G4P in
CC       creating zone through which the phage assembled and extruded (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Isoform G11P is also involved in phage assembly, probably
CC       playing a structural role in the formation of the phage assembly site.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G4P; this interaction results in a complex that
CC       spans the inner an outer host membranes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=G1P; Synonyms=Gene 1 protein;
CC         IsoId=P03655-1; Sequence=Displayed;
CC       Name=G11P; Synonyms=Gene 11 protein;
CC         IsoId=P03655-2; Sequence=VSP_037570;
CC   -!- SIMILARITY: Belongs to the inovirus G1P protein family. {ECO:0000305}.
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DR   EMBL; J02451; AAA32311.1; -; Genomic_DNA.
DR   PIR; A04262; Z1BPFD.
DR   RefSeq; YP_009111305.1; NC_025824.1. [P03655-1]
DR   GeneID; 22475006; -.
DR   KEGG; vg:22475006; -.
DR   Proteomes; UP000001836; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0099045; P:viral extrusion; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008900; Zot_N.
DR   Pfam; PF05707; Zot; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; ATP-binding; Host membrane; Membrane;
KW   Nucleotide-binding; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral extrusion; Viral release from host cell.
FT   CHAIN           1..348
FT                   /note="Gene 1 protein"
FT                   /id="PRO_0000098202"
FT   TOPO_DOM        1..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        253..273
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        274..348
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..240
FT                   /note="Missing (in isoform G11P)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037570"
SQ   SEQUENCE   348 AA;  39537 MW;  CDD5040792E244AD CRC64;
     MAVYFVTGKL GSGKTLVSVG KIQDKIVAGC KIATNLDLRL QNLPQVGRFA KTPRVLRIPD
     KPSISDLLAI GRGNDSYDEN KNGLLVLDEC GTWFNTRSWN DKERQPIIDW FLHARKLGWD
     IIFLVQDLSI VDKQARSALA EHVVYCRRLD RITLPFVGTL YSLVTGSKMP LPKLHVGVVK
     YGDSQLSPTV ERWLYTGKNL YNAYDTKQAF SSNYDSGVYS YLTPYLSHGR YFKPLNLGQK
     MKLTKIYLKK FSRVLCLAIG FASAFTYSYI TQPKPEVKKV VSQTYDFDKF TIDSSQRLNL
     SYRYVFKDSK GKLINSDDLQ KQGYSITYID LCTVSIKKGN SNEIVKCN