G4P_BPF1
ID G4P_BPF1 Reviewed; 426 AA.
AC P03666; Q96223;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Virion export protein;
DE AltName: Full=Gene 4 protein;
DE Short=G4P;
DE Flags: Precursor;
GN Name=IV;
OS Enterobacteria phage f1 (Bacteriophage f1).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=10863;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6282703; DOI=10.1016/0378-1119(81)90059-7;
RA Beck E., Zink B.;
RT "Nucleotide sequence and genome organisation of filamentous bacteriophages
RT f1 and fd.";
RL Gene 16:35-58(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6292494; DOI=10.1128/jvi.44.1.32-46.1982;
RA Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage f1 DNA.";
RL J. Virol. 44:32-46(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-426.
RX PubMed=439137; DOI=10.1016/0022-2836(79)90090-1;
RA Ravetch J.V., Horiuchi K., Zinder N.D.;
RT "DNA sequence analysis of the defective interfering particles of
RT bacteriophage f1.";
RL J. Mol. Biol. 128:305-318(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-399.
RA Grachev S.A., Kolosov M.N., Korobko V.G., Petrov N.A.;
RT "Nucleotide sequence of a gene IV fragment of bacteriophage f1.";
RL Bioorg. Khim. 4:569-570(1978).
RN [5]
RP INTERACTION WITH G1P.
RX PubMed=10564514; DOI=10.1046/j.1365-2958.1999.01636.x;
RA Feng J.N., Model P., Russel M.;
RT "A trans-envelope protein complex needed for filamentous phage assembly and
RT export.";
RL Mol. Microbiol. 34:745-755(1999).
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.
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; V00606; CAA23875.1; -; Genomic_DNA.
DR EMBL; J02448; AAA32218.1; -; Genomic_DNA.
DR EMBL; M10641; AAA32222.1; -; Genomic_DNA.
DR EMBL; M38348; AAA32221.1; ALT_SEQ; Genomic_DNA.
DR PIR; C04268; Z4BPF1.
DR PDB; 7OFH; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=22-426.
DR PDBsum; 7OFH; -.
DR SMR; P03666; -.
DR TCDB; 1.B.22.5.1; the outer bacterial membrane secretin (secretin) family.
DR Proteomes; UP000002557; Genome.
DR Proteomes; UP000241027; 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 1: Evidence at protein level;
KW 3D-structure; Host membrane; Membrane; 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_0000209448"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 30
FT /note="S -> P (in Ref. 2; AAA32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> N (in Ref. 2; AAA32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="I -> N (in Ref. 2; AAA32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="V -> I (in Ref. 2; AAA32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="V -> I (in Ref. 2; AAA32218)"
FT /evidence="ECO:0000305"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:7OFH"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:7OFH"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:7OFH"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:7OFH"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 268..278
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 283..294
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 312..327
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 355..367
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 369..381
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:7OFH"
FT STRAND 410..422
FT /evidence="ECO:0007829|PDB:7OFH"
SQ SEQUENCE 426 AA; 45842 MW; 27593CC35BAE610B CRC64;
MKLLNVINFV FLMFVSSSSF AQVIEMNNSS LRDFVTWYSK QTGESVIVSP DVKGTVTVYS
SDVKPENLRD FFISVLRANN FDMVGSIPSI IQKYNPNNQD YIDELPSSDN QEYDDNSAPS
GGFFVPQNDN VTQTFKINNV RAKDLIRVVE LFVKSNTSKS SNVLSVDGSN LLVVSAPKDI
LDNLPQFLST VDLPTDQILI EGLIFEVQQG DALDFSFAAG SQRGTVAGGV NTDRLTSVLS
SAGGSFGIFN GDVLGLSVRA LKTNSHSKIL SVPRILTLSG QKGSISVGQN VPFITGRVTG
ESANVNNPFQ TVERQNVGIS MSVFPVAMAG GNIVLDITSK ADSLSSSTQA SDVITNQRSI
ATTVNLRDGQ TLLLGGLTDY KNTSQDSGVP FLSKIPLIGL LFSSRSDSNE ESTLYVLVKA
TIVRAL
