ID   G3P_BPPHL               Reviewed;         367 AA.
AC   Q37972;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 59.
DE   RecName: Full=Attachment protein G3P;
DE   AltName: Full=Gene 3 protein;
DE            Short=G3P;
DE   AltName: Full=Minor coat protein;
GN   Name=III;
OS   Xanthomonas phage phiLf (Bacteriophage phi-Lf).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; unclassified Inoviridae.
OX   NCBI_TaxID=28365;
OH   NCBI_TaxID=340; Xanthomonas campestris pv. campestris.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8654978; DOI=10.1016/0378-1119(96)00197-7;
RA   Wen F.S., Tseng Y.H.;
RT   "Nucleotide sequence of the gene presumably encoding the adsorption protein
RT   of filamentous phage phi Lf.";
RL   Gene 172:161-162(1996).
CC   -!- FUNCTION: Plays essential roles both in the penetration of the viral
CC       genome into the bacterial host via pilus retraction and in the
CC       extrusion process. During the initial step of infection, G3P mediates
CC       adsorption of the phage to its primary receptor, the tip of host F-
CC       pilus. Subsequent interaction with the host entry receptor tolA induces
CC       penetration of the viral DNA into the host cytoplasm. In the extrusion
CC       process, G3P mediates the release of the membrane-anchored virion from
CC       the cell via its C-terminal domain (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G6P; this interaction is required for proper
CC       integration of G3P and G6P into the virion. Interacts with G8P (By
CC       similarity). Interacts with host tolA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Prior
CC       to assembly, G3P is found associated with the bacterial host inner
CC       membrane. There are about five copies of this protein per mature phage
CC       that are located on the head side of the filamentous virion.
CC   -!- SIMILARITY: Belongs to the inovirus G3P protein family. {ECO:0000305}.
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DR   EMBL; U10884; AAB87092.1; -; Genomic_DNA.
DR   PIR; JC4831; JC4831.
DR   SMR; Q37972; -.
DR   Proteomes; UP000007611; 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:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039667; P:viral entry into host cell via pilus retraction; IEA:UniProtKB-KW.
DR   GO; GO:0099045; P:viral extrusion; IEA:UniProtKB-KW.
DR   GO; GO:0039666; P:virion attachment to host cell pilus; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix;
KW   Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW   Viral attachment to host cell pilus;
KW   Viral attachment to host entry receptor; Viral extrusion;
KW   Viral penetration into host cytoplasm;
KW   Viral penetration into host cytoplasm via pilus retraction;
KW   Viral release from host cell; Virion; Virus entry into host cell.
FT   CHAIN           1..367
FT                   /note="Attachment protein G3P"
FT                   /id="PRO_0000378355"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          193..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..214
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  36736 MW;  66A50CDE693A990D CRC64;
     MSPSLFLGWG DDYFVVLWIH GRAVRLGRRQ GVGRVIRVSL AMLILLALTF SPIVHATCVQ
     TEPSTSANNG SWACSDQGEA FAKASSMGVP ADLSVCRMKS IRAVSSGPGV FSQRMTYPGD
     TCGIGYDLDI GTGNATYPDT ATCAKRPSQS GWTNPTAPTP SDVCNDGCYY TYAVDAGGPK
     GYTYVPSGAT CTTDDAAPPI DDGGDGDDDG GGDGGGDGGG DGGGDGGGDG GGDGGGDGGG
     DGGGDGGGDG DGGGDGDGDG DGDGDGEEGG EGAPMSELYK KSGKTVESVL SKFNTQVRGT
     PMVAGIGDFM KVPSGGSCPV FSLGASKWWD AMTINFHCGG DFLAFLRAAG WVILAIAAYA
     AIRIAVT