G3P_BPFD
ID G3P_BPFD Reviewed; 424 AA.
AC P03661;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 130.
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 Enterobacteria phage fd (Bacteriophage fd).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=2847073;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=478 / Heidelberg;
RX PubMed=745987; DOI=10.1093/nar/5.12.4495;
RA Beck E., Sommer R., Auerswald E.A., Kurz C., Zink B., Osterburg G.,
RA Schaller H., Sugimoto K., Sugisaki H., Okamoto T., Takanami M.;
RT "Nucleotide sequence of bacteriophage fd DNA.";
RL Nucleic Acids Res. 5:4495-4503(1978).
RN [2]
RP PROTEIN SEQUENCE OF 19-27.
RX PubMed=329863; DOI=10.1021/bi00631a016;
RA Goldsmith M.E., Konigsberg W.H.;
RT "Adsorption protein of the bacteriophage fd: isolation, molecular
RT properties, and location in the virus.";
RL Biochemistry 16:2686-2694(1977).
RN [3]
RP INTERACTION WITH HOST TOLA.
RX PubMed=9244308; DOI=10.1016/s0092-8674(00)80342-6;
RA Riechmann L., Holliger P.;
RT "The C-terminal domain of TolA is the coreceptor for filamentous phage
RT infection of E. coli.";
RL Cell 90:351-360(1997).
RN [4]
RP FUNCTION.
RX PubMed=12054858; DOI=10.1016/s0022-2836(02)00260-7;
RA Deng L.W., Perham R.N.;
RT "Delineating the site of interaction on the pIII protein of filamentous
RT bacteriophage fd with the F-pilus of Escherichia coli.";
RL J. Mol. Biol. 319:603-614(2002).
RN [5]
RP FUNCTION.
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).
RN [6]
RP STRUCTURE BY NMR OF 20-85.
RX PubMed=9032075; DOI=10.1016/s0969-2126(97)00184-6;
RA Holliger P., Riechmann L.;
RT "A conserved infection pathway for filamentous bacteriophages is suggested
RT by the structure of the membrane penetration domain of the minor coat
RT protein g3p from phage fd.";
RL Structure 5:265-275(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-235, AND DISULFIDE BONDS.
RX PubMed=10329170; DOI=10.1006/jmbi.1999.2720;
RA Holliger P., Riechmann L., Williams R.L.;
RT "Crystal structure of the two N-terminal domains of g3p from filamentous
RT phage fd at 1.9 A: evidence for conformational lability.";
RL J. Mol. Biol. 288:649-657(1999).
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. {ECO:0000269|PubMed:12054858,
CC ECO:0000269|PubMed:21110981}.
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. {ECO:0000250,
CC ECO:0000269|PubMed:9244308}.
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 -!- DOMAIN: Consists of three domains (N1, N2, and CT). The N2 domain
CC interacts with the F pilus, whereas the N1 domain forms a complex with
CC the C-terminal domain of tolA at later stages of the infection process.
CC N1 is connected to N2 by a flexible glycine-rich linker on the phage.
CC The C-terminal domain is required for release of viral particles from
CC the host bacterial membrane and proper integration of G3P and G6P
CC proteins in the virion.
CC -!- SIMILARITY: Belongs to the inovirus G3P protein family. {ECO:0000305}.
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DR EMBL; J02451; AAA32309.1; -; Genomic_DNA.
DR PIR; A04266; Z3BPFD.
DR RefSeq; YP_009111303.1; NC_025824.1.
DR PDB; 1FGP; NMR; -; A=20-85.
DR PDB; 2G3P; X-ray; 1.90 A; A/B=19-235.
DR PDB; 3DGS; X-ray; 1.90 A; A/B=19-235.
DR PDB; 3KNQ; X-ray; 2.13 A; A/B=19-240.
DR PDBsum; 1FGP; -.
DR PDBsum; 2G3P; -.
DR PDBsum; 3DGS; -.
DR PDBsum; 3KNQ; -.
DR SMR; P03661; -.
DR GeneID; 22475004; -.
DR KEGG; vg:22475004; -.
DR EvolutionaryTrace; P03661; -.
DR Proteomes; UP000001836; 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; IMP:CAFA.
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:0039668; P:viral entry into host cell via pilus basal pore; IMP:CAFA.
DR GO; GO:0099045; P:viral extrusion; IEA:UniProtKB-KW.
DR GO; GO:0039666; P:virion attachment to host cell pilus; IMP:CAFA.
DR Gene3D; 3.90.450.1; -; 1.
DR InterPro; IPR008021; Attachment_G3P_N.
DR InterPro; IPR036200; Attachment_G3P_N_sf.
DR InterPro; IPR013834; Phage_G3P_N2_sf.
DR Pfam; PF05357; Phage_Coat_A; 2.
DR SUPFAM; SSF50176; SSF50176; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing; Disulfide bond;
KW Host membrane; Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; 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..18
FT /evidence="ECO:0000269|PubMed:329863"
FT CHAIN 19..424
FT /note="Attachment protein G3P"
FT /id="PRO_0000003289"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 19..85
FT /note="N1"
FT REGION 83..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..104
FT /note="G1 (Gly-rich linker)"
FT REGION 105..235
FT /note="N2"
FT REGION 222..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..274
FT /note="G2 (Gly-rich linker)"
FT REGION 253..262
FT /note="Not essential for gene 3 function"
FT REGION 275..424
FT /note="CT"
FT COMPBIAS 128..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 25..54
FT /evidence="ECO:0000269|PubMed:10329170"
FT DISULFID 64..71
FT /evidence="ECO:0000269|PubMed:10329170"
FT DISULFID 206..219
FT /evidence="ECO:0000269|PubMed:10329170"
FT CONFLICT 25
FT /note="C -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="A -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1FGP"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:2G3P"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3DGS"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2G3P"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2G3P"
FT TURN 200..208
FT /evidence="ECO:0007829|PDB:2G3P"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2G3P"
SQ SEQUENCE 424 AA; 44638 MW; 1D2FE0343AB6B2F0 CRC64;
MKKLLFAIPL VVPFYSHSAE TVESCLAKPH TENSFTNVWK DDKTLDRYAN YEGCLWNATG
VVVCTGDETQ CYGTWVPIGL AIPENEGGGS EGGGSEGGGS EGGGTKPPEY GDTPIPGYTY
INPLDGTYPP GTEQNPANPN PSLEESQPLN TFMFQNNRFR NRQGALTVYT GTVTQGTDPV
KTYYQYTPVS SKAMYDAYWN GKFRDCAFHS GFNEDPFVCE YQGQSSDLPQ PPVNAGGGSG
GGSGGGSEGG GSEGGGSEGG GSEGGGSGGG SGSGDFDYEK MANANKGAMT ENADENALQS
DAKGKLDSVA TDYGAAIDGF IGDVSGLANG NGATGDFAGS NSQMAQVGDG DNSPLMNNFR
QYLPSLPQSV ECRPYVFGAG KPYEFSIDCD KINLFRGVFA FLLYVATFMY VFSTFANILR
NKES
