G3P_BPIF1
ID G3P_BPIF1 Reviewed; 460 AA.
AC O80297;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 02-JUN-2021, entry version 92.
DE RecName: Full=Attachment protein G3P;
DE AltName: Full=Gene 3 protein;
DE Short=G3P;
DE AltName: Full=Minor coat protein;
DE Flags: Precursor;
GN Name=III;
OS Escherichia phage If1 (Bacteriophage If1).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Infulavirus.
OX NCBI_TaxID=10868;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hill D.F., Hughes G., McNaughton J.C., Stockwell P.A., Petersen G.B.;
RT "DNA sequence of the filamentous coliphage If1.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 17-81.
RX PubMed=21110981; DOI=10.1016/j.jmb.2010.11.030;
RA Lorenz S.H., Jakob R.P., Weininger U., Balbach J., Dobbek H., Schmid F.X.;
RT "The filamentous phages fd and IF1 use different mechanisms to infect
RT Escherichia coli.";
RL J. Mol. Biol. 405:989-1003(2011).
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 I-
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 type I membrane protein {ECO:0000305}.
CC Note=Prior to assembly, G3P is found associated with the bacterial host
CC inner membrane. There are about five copies of this protein per mature
CC phage 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; U02303; AAC62155.1; -; Genomic_DNA.
DR RefSeq; NP_047356.1; NC_001954.1.
DR PDB; 2X9A; X-ray; 2.47 A; A/C=17-81.
DR PDB; 2X9B; X-ray; 2.92 A; A/B=17-81.
DR PDBsum; 2X9A; -.
DR PDBsum; 2X9B; -.
DR SMR; O80297; -.
DR GeneID; 1261855; -.
DR KEGG; vg:1261855; -.
DR EvolutionaryTrace; O80297; -.
DR Proteomes; UP000001833; 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:0019028; C:viral capsid; 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.
DR InterPro; IPR008021; Attachment_G3P_N.
DR InterPro; IPR036200; Attachment_G3P_N_sf.
DR Pfam; PF05357; Phage_Coat_A; 1.
DR SUPFAM; SSF50176; SSF50176; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Disulfide bond; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
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 SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..460
FT /note="Attachment protein G3P"
FT /id="PRO_0000003291"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 76..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 23..50
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:2X9A"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2X9A"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2X9A"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2X9A"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:2X9A"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2X9A"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:2X9A"
SQ SEQUENCE 460 AA; 48790 MW; 9AD651968C715AB2 CRC64;
MKKIIIALFF APFFTHATTD AECLSKPAFD GTLSNVWKEG DSRYANFENC IYELSGIGIG
YDNDTSCNGH WTPVRAADGS GNGGDDNSSG GGSNGDSGNN STPDTVTPGQ TVNLPSDLST
LSIPANVVKS DSIGSQFSLY TNASCTMCSG YYLSNNADSI AIANITETVK ADYNQPDMWF
EQTDSDGNHV KILQNSYKAV SYNVESKQSD VNNPTYINYS YSVNVKQVSY DTSNVCIMNW
ETFQNKCDAS RAVLITDTVT PSYSRNITIQ SNINYQGSNG SGGSGGSGGS GNDGGGTGNN
GNGTGDFDYV KMANANKDAL TESFDLSALQ ADTGASLDGS VQGTLDSLSG FSDSIGGLVG
NGSAISGEFA GSSAAMNAIG EGDKSPLLDS LSFLKDGLFP ALPEFKQCTP FVFAPGKEYE
FIIECKYIDM FKGIFAFILY FWTFVTVYDS FSGILRKGRG
