G4P_BPIKE
ID G4P_BPIKE Reviewed; 437 AA.
AC P03667;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 96.
DE RecName: Full=Virion export protein;
DE AltName: Full=Gene 4 protein;
DE Short=G4P;
DE Flags: Precursor;
GN Name=IV;
OS Salmonella phage IKe (Bacteriophage IKe).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Lineavirus.
OX NCBI_TaxID=10867;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3981635; DOI=10.1016/0022-2836(85)90322-5;
RA Peeters B.P.H., Peters R.M., Schoenmakers J.G.G., Konings R.N.H.;
RT "Nucleotide sequence and genetic organization of the genome of the N-
RT specific filamentous bacteriophage IKe. Comparison with the genome of the
RT F-specific filamentous phages M13, fd and f1.";
RL J. Mol. Biol. 181:27-39(1985).
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; X02139; CAA26076.1; -; Genomic_DNA.
DR PIR; A04269; Z4BPIK.
DR RefSeq; NP_040579.1; NC_002014.1.
DR SMR; P03667; -.
DR GeneID; 1260883; -.
DR KEGG; vg:1260883; -.
DR Proteomes; UP000000372; 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..437
FT /note="Virion export protein"
FT /id="PRO_0000209452"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 99..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 46486 MW; D2456EF357F0D819 CRC64;
MKLQAEKKLI FGYVALCFLM TLGIAFNVLA DPVNLNNAPV RSFVQWYSQK SNKAVVVNPD
VKGNITVFNA DVNQANIDDF FKSVLNANGF VLMAGDPSGV STPSKLPSQQ TDNDDDYEDS
ADYVPVGDSV PVSAQPQKPL DLTVRNFKLT RVRSSDVLPL AKIFVDSNGG GDVIDYPGNN
SLLVSGSAAI MNALADFITS IDVARDQVLI QSLMFETSLV NGVDLSFAAG SASGDKVAGG
FNTSALGTAL STAGGSFGIF NGNVLALSIQ AVKNDSNSKV ISTPRILTQS GQTGYISVGQ
NVPFVTGKVT GEAANVNNPF QTIERRDVGV SLKVTPVVMG NGQLVLTIDT KADSLTSQMT
ASDIITNQRH MQTTVQIKDG QTLLLGGLID SNTTDGNRSV PWFESVPVIG WLFRSHSDSH
NERTMFVLLT AHVIKAL
