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 18-SEP-2019, entry version 79. 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 RT of membrane potential."; RL J. Biol. Chem. 263:11575-11583(1988). CC -!- FUNCTION: Isoform G1P plays an essential role in phage assembly. CC It is required to increase the number of adhesion zones between CC the inner and outer membranes of the host cell. The extrusion of CC neo-synthesized phages occurs at these adhesion sites. May be CC involved with G4P in creating zone through which the phage CC assembled and extruded (By similarity). {ECO:0000250}. CC -!- FUNCTION: Isoform G11P is also involved in phage assembly, CC probably playing a structural role in the formation of the phage CC assembly site. {ECO:0000250}. CC -!- SUBUNIT: Interacts with G4P; this interaction results in a complex CC that spans the inner an outer host membranes. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass CC membrane 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. CC {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; Complete proteome; Host membrane; KW Membrane; Nucleotide-binding; Reference proteome; Signal-anchor; KW Transmembrane; Transmembrane helix; Viral extrusion; KW Viral release from host cell. FT CHAIN 1 348 Gene 1 protein. FT /FTId=PRO_0000098202. FT TOPO_DOM 1 252 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 253 273 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000305}. FT TOPO_DOM 274 348 Periplasmic. {ECO:0000305}. FT NP_BIND 8 15 ATP. {ECO:0000255}. FT VAR_SEQ 1 240 Missing (in isoform G11P). {ECO:0000305}. FT /FTId=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 //