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 11-DEC-2019, entry version 81. DE RecName: Full=Gene 1 protein; DE AltName: Full=G1P; GN Name=I; OS Enterobacteria phage fd (Bacteriophage fd). OC Viruses; Inoviridae; Inovirus; unclassified Inovirus. OX NCBI_TaxID=10864; 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; 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}. 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; J02451; AAA32311.1; -; Genomic_DNA. DR PIR; A04262; Z1BPFD. DR RefSeq; YP_009111305.1; NC_025824.1. [P03655-1] DR PRIDE; P03655; -. 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 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 NP_BIND 8..15 FT /note="ATP" 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 //