ID   G4P_BPIF1               Reviewed;         429 AA.
AC   O80300;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   07-APR-2021, entry version 80.
DE   RecName: Full=Virion export protein;
DE   AltName: Full=Gene 4 protein;
DE            Short=G4P;
DE   Flags: Precursor;
GN   Name=IV;
OS   Escherichia phage If1 (Bacteriophage If1).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Infulavirus.
OX   NCBI_TaxID=10868;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hill D.F., Hughes G., McNaughton J.C., Stockwell P.A., Petersen G.B.;
RT   "DNA sequence of the filamentous coliphage If1.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts in the assembly and extrusion of the bacteriophage by
CC       forming a channel across the host outer membrane. This channel is just
CC       large enough to allow a newly synthesized phage particle to pass
CC       through. Extrusion is a process of concomitant assembly and secretion
CC       and takes place at specific assembly sites where host inner and outer
CC       membranes are in close contacts (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer. The channel is composed of 14 G4P subunits that
CC       confer a barrel-like structure. Interacts with G1P; this interaction
CC       results in a complex that spans the inner an outer host membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the inovirus G4P protein family. {ECO:0000305}.
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DR   EMBL; U02303; AAC62158.1; -; Genomic_DNA.
DR   RefSeq; NP_047359.1; NC_001954.1.
DR   SMR; O80300; -.
DR   GeneID; 1261858; -.
DR   KEGG; vg:1261858; -.
DR   Proteomes; UP000001833; 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:0009306; P:protein secretion; IEA:InterPro.
DR   GO; GO:0099045; P:viral extrusion; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1370.120; -; 1.
DR   InterPro; IPR001775; GspD/PilQ.
DR   InterPro; IPR038591; NolW-like_sf.
DR   InterPro; IPR004846; T2SS/T3SS.
DR   InterPro; IPR004845; T2SS_GspD_CS.
DR   Pfam; PF00263; Secretin; 1.
DR   PRINTS; PR00811; BCTERIALGSPD.
DR   PROSITE; PS00875; T2SP_D; 1.
PE   3: Inferred from homology;
KW   Host membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Viral extrusion; Viral release from host cell.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..429
FT                   /note="Virion export protein"
FT                   /id="PRO_0000209451"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   429 AA;  45863 MW;  917DB3B75C3915C5 CRC64;
     MKKLLASLLC VLSFQSFAIP VELNNAPVRE FVSWYSKTTG KPVIISPDVK GEITVYSADV
     TKDELPQFFT SVLRANGFDL SPGNPAVVQK FNRNTYEYSD SFSEPVPASS YDGDVPPPTG
     DFFTKPEIRA NLITQTYPVN NVRAKDLAPV IDIFLKGENI AGTKVYPLMG RIFLLVTASA
     SQHKELAAFF PSVDVPRTQV LVESVIFETT ASDGFDFSFA AGDPSGSPVA GGINTDRLTS
     VLSSTGGSFG IFNGNILGLS LKALETSSKS TLLSMPRILT MSGQPGTFTA GQNVPFVTGR
     VTGEAANVNN PFQTIERHDV GISLKVVPVV TPGGLLIMDV STNADSISDS QTASDIITNT
     RSISTTVQLK SGQTVLLGGM VDNRESDSDS SVPWVSKIPL IGALFTSKSS NANKRTLYIL
     IRARVVNLL