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Protein

Attachment protein G3P

Gene

III

Organism
Enterobacteria phage fd (Bacteriophage fd)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry receptor tolA induces penetration of the viral DNA into the host cytoplasm. In the extrusion process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral attachment to host adhesion receptor, Viral attachment to host cell, Viral attachment to host cell pilus, Viral attachment to host entry receptor, Viral extrusion, Viral penetration into host cytoplasm, Viral penetration into host cytoplasm via pilus retraction, Virus entry into host cell, Virus exit from host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Attachment protein G3P
Alternative name(s):
Gene 3 protein
Short name:
G3P
Minor coat protein
Gene namesi
Name:III
OrganismiEnterobacteria phage fd (Bacteriophage fd)
Taxonomic identifieri10864 [NCBI]
Taxonomic lineageiVirusesssDNA virusesInoviridaeInovirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000001836 Componenti: Genome

Subcellular locationi

  • Virion Curated
  • Host membrane Curated; Single-pass type I membrane protein Curated

  • Note: Prior to assembly, G3P is found associated with the bacterial host inner membrane. There are about five copies of this protein per mature phage that are located on the head side of the filamentous virion.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei398 – 41821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 424406Attachment protein G3PPRO_0000003289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 541 Publication
Disulfide bondi64 ↔ 711 Publication
Disulfide bondi206 ↔ 2191 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Interacts with G6P; this interaction is required for proper integration of G3P and G6P into the virion. Interacts with G8P (By similarity). Interacts with host tolA.By similarity1 Publication

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 276Combined sources
Beta strandi31 – 377Combined sources
Beta strandi39 – 413Combined sources
Turni42 – 443Combined sources
Beta strandi47 – 515Combined sources
Beta strandi54 – 6411Combined sources
Beta strandi66 – 694Combined sources
Beta strandi71 – 8010Combined sources
Helixi83 – 853Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi125 – 1284Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi142 – 1465Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi165 – 17511Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi181 – 1888Combined sources
Helixi192 – 1998Combined sources
Turni200 – 2089Combined sources
Beta strandi225 – 2284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FGPNMR-A20-85[»]
2G3PX-ray1.90A/B19-235[»]
3DGSX-ray1.90A/B19-235[»]
3KNQX-ray2.13A/B19-240[»]
DisProtiDP00034.
ProteinModelPortaliP03661.
SMRiP03661. Positions 20-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03661.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 8567N1Add
BLAST
Regioni86 – 10419G1 (Gly-rich linker)Add
BLAST
Regioni105 – 235131N2Add
BLAST
Regioni236 – 27439G2 (Gly-rich linker)Add
BLAST
Regioni253 – 26210Not essential for gene 3 function
Regioni275 – 424150CTAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi236 – 27439Gly-richAdd
BLAST

Domaini

Consists of three domains (N1, N2, and CT). The N2 domain interacts with the F pilus, whereas the N1 domain forms a complex with the C-terminal domain of tolA at later stages of the infection process. N1 is connected to N2 by a flexible glycine-rich linker on the phage. The C-terminal domain is required for release of viral particles from the host bacterial membrane and proper integration of G3P and G6P proteins in the virion.

Sequence similaritiesi

Belongs to the inovirus G3P protein family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.450.1. 1 hit.
InterProiIPR008021. Attachment_G3P_N.
IPR013834. Phage_G3P_N2.
[Graphical view]
PfamiPF05357. Phage_Coat_A. 2 hits.
[Graphical view]
SUPFAMiSSF50176. SSF50176. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03661-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLLFAIPL VVPFYSHSAE TVESCLAKPH TENSFTNVWK DDKTLDRYAN
60 70 80 90 100
YEGCLWNATG VVVCTGDETQ CYGTWVPIGL AIPENEGGGS EGGGSEGGGS
110 120 130 140 150
EGGGTKPPEY GDTPIPGYTY INPLDGTYPP GTEQNPANPN PSLEESQPLN
160 170 180 190 200
TFMFQNNRFR NRQGALTVYT GTVTQGTDPV KTYYQYTPVS SKAMYDAYWN
210 220 230 240 250
GKFRDCAFHS GFNEDPFVCE YQGQSSDLPQ PPVNAGGGSG GGSGGGSEGG
260 270 280 290 300
GSEGGGSEGG GSEGGGSGGG SGSGDFDYEK MANANKGAMT ENADENALQS
310 320 330 340 350
DAKGKLDSVA TDYGAAIDGF IGDVSGLANG NGATGDFAGS NSQMAQVGDG
360 370 380 390 400
DNSPLMNNFR QYLPSLPQSV ECRPYVFGAG KPYEFSIDCD KINLFRGVFA
410 420
FLLYVATFMY VFSTFANILR NKES
Length:424
Mass (Da):44,638
Last modified:July 21, 1986 - v1
Checksum:i1D2FE0343AB6B2F0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251C → P AA sequence (PubMed:329863).Curated
Sequence conflicti27 – 271A → P AA sequence (PubMed:329863).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02451 Genomic DNA. Translation: AAA32309.1.
PIRiA04266. Z3BPFD.
RefSeqiYP_009111303.1. NC_025824.1.

Genome annotation databases

GeneIDi22475004.
KEGGivg:22475004.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02451 Genomic DNA. Translation: AAA32309.1.
PIRiA04266. Z3BPFD.
RefSeqiYP_009111303.1. NC_025824.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FGPNMR-A20-85[»]
2G3PX-ray1.90A/B19-235[»]
3DGSX-ray1.90A/B19-235[»]
3KNQX-ray2.13A/B19-240[»]
DisProtiDP00034.
ProteinModelPortaliP03661.
SMRiP03661. Positions 20-234.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi22475004.
KEGGivg:22475004.

Miscellaneous databases

EvolutionaryTraceiP03661.

Family and domain databases

Gene3Di3.90.450.1. 1 hit.
InterProiIPR008021. Attachment_G3P_N.
IPR013834. Phage_G3P_N2.
[Graphical view]
PfamiPF05357. Phage_Coat_A. 2 hits.
[Graphical view]
SUPFAMiSSF50176. SSF50176. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 478 / Heidelberg.
  2. "Adsorption protein of the bacteriophage fd: isolation, molecular properties, and location in the virus."
    Goldsmith M.E., Konigsberg W.H.
    Biochemistry 16:2686-2694(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-27.
  3. "The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli."
    Riechmann L., Holliger P.
    Cell 90:351-360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST TOLA.
  4. "Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli."
    Deng L.W., Perham R.N.
    J. Mol. Biol. 319:603-614(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The filamentous phages fd and IF1 use different mechanisms to infect Escherichia coli."
    Lorenz S.H., Jakob R.P., Weininger U., Balbach J., Dobbek H., Schmid F.X.
    J. Mol. Biol. 405:989-1003(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd."
    Holliger P., Riechmann L.
    Structure 5:265-275(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 20-85.
  7. "Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability."
    Holliger P., Riechmann L., Williams R.L.
    J. Mol. Biol. 288:649-657(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-235, DISULFIDE BONDS.

Entry informationi

Entry nameiG3P_BPFD
AccessioniPrimary (citable) accession number: P03661
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 14, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.