G3P_BPM13
ID G3P_BPM13 Reviewed; 424 AA.
AC P69168; P03662;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 29-SEP-2021, entry version 91.
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 M13 (Bacteriophage M13).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=1977402;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6254849; DOI=10.1016/0378-1119(80)90093-1;
RA van Wezenbeek P.M.G.F., Hulsebos T.J.M., Schoenmakers J.G.G.;
RT "Nucleotide sequence of the filamentous bacteriophage M13 DNA genome:
RT comparison with phage fd.";
RL Gene 11:129-148(1980).
RN [2]
RP INTERACTION WITH PROTEIN G6P.
RX PubMed=7746960; DOI=10.1016/0923-2508(94)90042-6;
RA Gailus V., Ramsperger U., Johner C., Kramer H., Rasched I.;
RT "The role of the adsorption complex in the termination of filamentous phage
RT assembly.";
RL Res. Microbiol. 145:699-709(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 19-235.
RX PubMed=9461080; DOI=10.1038/nsb0298-140;
RA Lubkowski J., Hennecke F., Plueckthun A., Wlodawer A.;
RT "The structural basis of phage display elucidated by the crystal structure
RT of the N-terminal domains of g3p.";
RL Nat. Struct. Biol. 5:140-147(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-105 IN COMPLEX WITH TOLA.
RX PubMed=10404600; DOI=10.1016/s0969-2126(99)80092-6;
RA Lubkowski J., Hennecke F., Plueckthun A., Wlodawer A.;
RT "Filamentous phage infection: crystal structure of g3p in complex with its
RT coreceptor, the C-terminal domain of TolA.";
RL Structure 7:711-722(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.
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. Host membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}. Note=Prior to assembly, G3P is
CC found associated with the bacterial host inner membrane. There are
CC about five copies of this protein per mature phage that are located on
CC 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 -!- PTM: In one of the crystallographic structures Trp-39 is oxidized to
CC 1',2'-dihydro-2'-oxotryptophan. {ECO:0000269|PubMed:9461080}.
CC -!- SIMILARITY: Belongs to the inovirus G3P protein family. {ECO:0000305}.
CC -!- CAUTION: The oxidation form of Trp-39 is subject of controversy and
CC could be the artifactual result of sample handling.
CC {ECO:0000305|PubMed:9461080}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V00604; CAA23862.1; -; Genomic_DNA.
DR PIR; C04266; Z3BPM3.
DR PDB; 1G3P; X-ray; 1.46 A; A=19-235.
DR PDB; 1TOL; X-ray; 1.85 A; A=19-104.
DR PDBsum; 1G3P; -.
DR PDBsum; 1TOL; -.
DR SMR; P69168; -.
DR EvolutionaryTrace; P69168; -.
DR Proteomes; UP000002111; 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 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; 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..18
FT CHAIN 19..424
FT /note="Attachment protein G3P"
FT /id="PRO_0000003293"
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 DISULFID 64..71
FT DISULFID 206..219
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1G3P"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 68..80
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:1G3P"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1G3P"
FT TURN 200..206
FT /evidence="ECO:0007829|PDB:1G3P"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1G3P"
SQ SEQUENCE 424 AA; 44652 MW; 764E2B599B66A2A1 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 ECRPFVFSAG KPYEFSIDCD KINLFRGVFA FLLYVATFMY VFSTFANILR
NKES
