G3P_BPIKE
ID G3P_BPIKE Reviewed; 434 AA.
AC P03663;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 103.
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 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: 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 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; X02139; CAA26073.1; -; Genomic_DNA.
DR PIR; A04267; Z3BPIK.
DR RefSeq; NP_040576.1; NC_002014.1.
DR PDB; 4EO0; X-ray; 1.61 A; A=20-127.
DR PDB; 4EO1; X-ray; 1.80 A; A=130-199.
DR PDBsum; 4EO0; -.
DR PDBsum; 4EO1; -.
DR SMR; P03663; -.
DR TCDB; 1.B.53.1.3; the filamentous phage g3p channel-forming protein (fp-g3p) family.
DR GeneID; 1260884; -.
DR KEGG; vg:1260884; -.
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: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; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Signal; 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..19
FT CHAIN 20..434
FT /note="Attachment protein G3P"
FT /id="PRO_0000003292"
FT TRANSMEM 408..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 191..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:4EO0"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4EO0"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:4EO0"
FT HELIX 56..84
FT /evidence="ECO:0007829|PDB:4EO0"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4EO0"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4EO0"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4EO0"
FT STRAND 112..124
FT /evidence="ECO:0007829|PDB:4EO0"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:4EO1"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4EO1"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4EO1"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4EO1"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4EO1"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:4EO1"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:4EO1"
SQ SEQUENCE 434 AA; 45575 MW; 22AC4E03F9AF4D86 CRC64;
MKRKIIAISL FLYIPLSNAD NWESITKSYY TGFAISKTVE SKDKDGKPVR KEVITQADLT
TACNDAKASA QNVFNQIKLT LSGTWPNSQF RLVTGDTCVY NGSPGEKTES WSIRAQVEGD
IQRSVPDEEP SEQTPEEICE AKPPIDGVFN NVFKGDEGGF YINYNGCEYE ATGVTVCQND
GTVCSSSAWK PTGYVPESGE PSSSPLKDGD TGGTGEGGSD TGGDTGGGDT GGGSTGGDTG
GSSGGGSSGG GSSGGSTGKS LTKEDVTAAI HVASPSIGDA VKDSLTEDND QYDNQKKADE
QSAKASASVS DAISDGMRGV GNFVDDFGGE SSQYGTGNSE MDLSVSLAKG QLGIDREGHG
SAWESFLNDG ALRPSIPTGH GCTNFVMYQG SVYQIEIGCD KLNDIKSVLS WVMYCLTFWY
VFQSVTSLLR KGEQ
