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Protein

Portal protein

Gene

10

Organism
Bacillus phage phi29 (Bacteriophage phi-29)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the packaging RNA (pRNA) and ATPase gp16 motor (PubMed:15886394).1 Publication1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Viral short tail ejection system

Keywords - Biological processi

Viral capsid assembly, Viral genome ejection through host cell envelope, Viral genome packaging, Viral penetration into host cytoplasm, Virus entry into host cell, Virus exit from host cell

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Portal protein
Alternative name(s):
Gene product 10
Short name:
gp10
Head-to-tail connector
Upper collar protein
Gene namesi
Name:10
OrganismiBacillus phage phi29 (Bacteriophage phi-29)
Taxonomic identifieri10756 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaePhi29likevirus
Virus hostiBacillus subtilis [TaxID: 1423]

Subcellular locationi

GO - Cellular componenti

  • viral procapsid Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Portal proteinPRO_0000106586Add
BLAST

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homododecamer.3 Publications

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Helixi18 – 3619Combined sources
Beta strandi38 – 436Combined sources
Helixi50 – 6011Combined sources
Beta strandi61 – 688Combined sources
Turni69 – 713Combined sources
Beta strandi72 – 765Combined sources
Beta strandi78 – 825Combined sources
Beta strandi86 – 883Combined sources
Beta strandi92 – 965Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi118 – 1247Combined sources
Helixi131 – 15424Combined sources
Beta strandi159 – 1635Combined sources
Helixi166 – 1683Combined sources
Helixi171 – 1766Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi195 – 2006Combined sources
Helixi207 – 22418Combined sources
Helixi247 – 27226Combined sources
Beta strandi277 – 2815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOUX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L1-309[»]
1H5WX-ray2.10A/B/C1-309[»]
1IJGX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-309[»]
1JNBX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L1-309[»]
1L4Pmodel-G/H/I/J/K/L/M/N/O/P/Q/R1-309[»]
1VRImodel-1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z1-309[»]
1VRJmodel-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j1-309[»]
1YWEmodel-1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z1-309[»]
ProteinModelPortaliP04332.
SMRiP04332. Positions 11-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04332.

Family & Domainsi

Family and domain databases

InterProiIPR008016. Gp10.
[Graphical view]
PfamiPF05352. Phage_connector. 1 hit.
[Graphical view]
ProDomiPD017810. Upper_collar_prot_phg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56826. SSF56826. 1 hit.

Sequencei

Sequence statusi: Complete.

P04332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKRSNTYR SINEIQRQKR NRWFIHYLNY LQSLAYQLFE WENLPPTINP
60 70 80 90 100
SFLEKSIHQF GYVGFYKDPV ISYIACNGAL SGQRDVYNQA TVFRAASPVY
110 120 130 140 150
QKEFKLYNYR DMKEEDMGVV IYNNDMAFPT TPTLELFAAE LAELKEIISV
160 170 180 190 200
NQNAQKTPVL IRANDNNQLS LKQVYNQYEG NAPVIFAHEA LDSDSIEVFK
210 220 230 240 250
TDAPYVVDKL NAQKNAVWNE MMTFLGIKNA NLEKKERMVT DEVSSNDEQI
260 270 280 290 300
ESSGTVFLKS REEACEKINE LYGLNVKVKF RYDIVEQMRR ELQQIENVSR

GTSDGETNE
Length:309
Mass (Da):35,878
Last modified:March 20, 1987 - v1
Checksum:iF5B01C1BE17FDE60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14782 Genomic DNA. Translation: AAA32283.1.
M12456 Genomic DNA. Translation: AAA32292.1.
PIRiE25816. WMBPC9.
RefSeqiYP_002004539.1. NC_011048.1.

Genome annotation databases

GeneIDi6446518.
KEGGivg:6446518.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14782 Genomic DNA. Translation: AAA32283.1.
M12456 Genomic DNA. Translation: AAA32292.1.
PIRiE25816. WMBPC9.
RefSeqiYP_002004539.1. NC_011048.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOUX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L1-309[»]
1H5WX-ray2.10A/B/C1-309[»]
1IJGX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-309[»]
1JNBX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L1-309[»]
1L4Pmodel-G/H/I/J/K/L/M/N/O/P/Q/R1-309[»]
1VRImodel-1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z1-309[»]
1VRJmodel-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j1-309[»]
1YWEmodel-1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z1-309[»]
ProteinModelPortaliP04332.
SMRiP04332. Positions 11-285.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6446518.
KEGGivg:6446518.

Miscellaneous databases

EvolutionaryTraceiP04332.

Family and domain databases

InterProiIPR008016. Gp10.
[Graphical view]
PfamiPF05352. Phage_connector. 1 hit.
[Graphical view]
ProDomiPD017810. Upper_collar_prot_phg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56826. SSF56826. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the late region of Bacillus phage phi 29 completes the 19,285-bp sequence of phi 29 genome. Comparison with the homologous sequence of phage PZA."
    Vlcek C., Paces V.
    Gene 46:215-225(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, nucleotide sequence and high level expression of the gene coding for the connector protein of Bacillus subtilis phage phi 29."
    Garcia J.A., Mendez E., Salas M.
    Gene 30:87-98(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Topology of the components of the DNA packaging machinery in the phage phi29 prohead."
    Ibarra B., Caston J.R., Llorca O., Valle M., Valpuesta J.M., Carrascosa J.L.
    J. Mol. Biol. 298:807-815(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Binding of pRNA to the N-terminal 14 amino acids of connector protein of bacteriophage phi29."
    Xiao F., Moll W.D., Guo S., Guo P.
    Nucleic Acids Res. 33:2640-2649(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACKAGING RNA.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), SUBUNIT.
  6. "Structure determination of the head-tail connector of bacteriophage phi29."
    Simpson A.A., Leiman P.G., Tao Y., He Y., Badasso M.O., Jardine P.J., Anderson D.L., Rossmann M.G.
    Acta Crystallogr. D 57:1260-1269(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), SUBUNIT.
  7. "Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle."
    Guasch A., Pous J., Ibarra B., Gomis-Ruth F.X., Valpuesta J.M., Sousa N., Carrascosa J.L., Coll M.
    J. Mol. Biol. 315:663-676(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiPORTL_BPPH2
AccessioniPrimary (citable) accession number: P04332
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: June 24, 2015
This is version 73 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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 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.