ID   G4P_BPM13               Reviewed;         426 AA.
AC   P03665;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Virion export protein;
DE   AltName: Full=Gene 4 protein;
DE            Short=G4P;
DE   Flags: Precursor;
GN   Name=IV;
OS   Enterobacteria phage M13 (Bacteriophage M13).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Inovirus.
OX   NCBI_TaxID=1977402;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6254849; DOI=10.1016/0378-1119(80)90093-1;
RA   van Wezenbeek P.M.G.F., Hulsebos T.J.M., Schoenmakers J.G.G.;
RT   "Nucleotide sequence of the filamentous bacteriophage M13 DNA genome:
RT   comparison with phage fd.";
RL   Gene 11:129-148(1980).
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; V00604; CAA23865.1; -; Genomic_DNA.
DR   PIR; B04268; Z4BPM3.
DR   SMR; P03665; -.
DR   PRIDE; P03665; -.
DR   Proteomes; UP000002111; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..426
FT                   /note="Virion export protein"
FT                   /id="PRO_0000209453"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   426 AA;  45865 MW;  AFA10978E2ACCC98 CRC64;
     MKLLNVINFV FLMFVSSSSF AQVIEMNNSP LRDFVTWYSK QSGESVIVSP DVKGTVTVYS
     SDVKPENLRN FFISVLRANN FDMVGSIPSI IQKYNPNNQD YIDELPSSDN QEYDDNSAPS
     GGFFVPQNDN VTQTFKINNV RAKDLIRVVE LFVKSNTSKS SNVLSIDGSN LLVVSAPKDI
     LDNLPQFLST VDLPTDQILI EGLIFEVQQG DALDFSFAAG SQRGTVAGGV NTDRLTSVLS
     SAGGSFGIFN GDVLGLSVRA LKTNSHSKIL SVPRILTLSG QKGSISVGQN VPFITGRVTG
     ESANVNNPFQ TIERQNVGIS MSVFPVAMAG GNIVLDITSK ADSLSSSTQA SDVITNQRSI
     ATTVNLRDGQ TLLLGGLTDY KNTSQDSGVP FLSKIPLIGL LFSSRSDSNE ESTLYVLVKA
     TIVRAL