ID   G4P_BPI22               Reviewed;         428 AA.
AC   P15420;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   12-AUG-2020, entry version 93.
DE   RecName: Full=Virion export protein;
DE   AltName: Full=Gene 4 protein;
DE            Short=G4P;
DE   Flags: Precursor;
GN   Name=IV;
OS   Enterobacteria phage I2-2 (Bacteriophage I2-2).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Lineavirus.
OX   NCBI_TaxID=10869;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schoenmakers H.F.P.M., Yu M., Konings R.N.H.;
RL   Submitted (FEB-1989) 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; X14336; CAA32520.1; -; Genomic_DNA.
DR   PIR; S08084; S08084.
DR   RefSeq; NP_039614.1; NC_001332.1.
DR   SMR; P15420; -.
DR   GeneID; 1260716; -.
DR   KEGG; vg:1260716; -.
DR   Proteomes; UP000000373; 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; IPR005644; NolW-like.
DR   InterPro; IPR038591; NolW-like_sf.
DR   InterPro; IPR004846; T2SS/T3SS.
DR   InterPro; IPR004845; T2SS_GspD_CS.
DR   Pfam; PF00263; Secretin; 1.
DR   Pfam; PF03958; Secretin_N; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..428
FT                   /note="Virion export protein"
FT                   /id="PRO_0000209450"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   428 AA;  45252 MW;  DA0A4E9103A38A42 CRC64;
     MKTFFAKFIV ALFAFTYFSA FAEPVTLNNS PVRSFVQWYS SKTGKSVIVN PDVKGNITVF
     NADVNNANID DFFKSVLNAN GLVVVAGNPA VVSTPLTKLA SQPSNEETYD DESDGVAYEA
     VPQSAAPAVP ADLTVRNFNV TRVRSSDVLP LAKIFVDSNG GGNVVDYPGN NSLVVSGSAQ
     VMPALSDFIT SIDVAREQVL IQSLMFETSV SNGVDLSFAL ALASGGKVAG GFNTSALGTA
     LSTAGGSFGI FNGNILALSL QAVQSDSNSK VISTPRILTQ SGQSGYISVG QNVPFVTGKV
     TGEAASVNNP FQTIERRDVG VSLKVTPVVM GNGQLVLTID TKADSLSNQA IASDIITNQR
     QIQTTVQIKD GQTLLLGGLI SSNQFDSDRS VPFMSKIPLI GWLFRSHSDS KDDRTMFVLL
     TAHVIRAL