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Protein

Baseplate hub protein gp27

Gene

27

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Baseplate protein that is part of the baseplate hub. Involved in the tail assembly.1 Publication1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Viral tail assembly, Virus exit from host cell

Protein family/group databases

TCDBi1.K.1.1.1. the gp27/5 t4-baseplate (t4-bp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Baseplate hub protein gp27Curated
Alternative name(s):
Gene product 27
Short name:
gp27
Hub protein 27
Gene namesi
Name:27
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000009087 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • virion Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Viral baseplate protein, Viral tail protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Baseplate hub protein gp27PRO_0000165015Add
BLAST

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.Curated

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homotrimer (PubMed:12837775, PubMed:19896486, PubMed:11823865). Interacts with gp5 trimer; this interaction forms the tail lysozyme complex (PubMed:12837775). The T4 tail lysozyme complex is made up of three copies of the proteolytically processed gp5 and three copies of gp27. Part of the baseplate macromolecular complex which consists of gp5, gp26, gp27, gp28, gp29 (hub); gp6, gp7, gp8, gp10, gp11, gp25, gp53 (wedge); gp9, gp12, gp48 and gp54.1 Publication3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
5P160092EBI-1032762,EBI-1032754

Protein-protein interaction databases

IntActiP17172. 1 interaction.
MINTiMINT-231925.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 208Combined sources
Helixi21 – 244Combined sources
Beta strandi32 – 4312Combined sources
Beta strandi48 – 547Combined sources
Helixi60 – 623Combined sources
Beta strandi69 – 746Combined sources
Beta strandi76 – 783Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi105 – 1106Combined sources
Helixi112 – 1154Combined sources
Helixi128 – 13912Combined sources
Turni140 – 1467Combined sources
Beta strandi149 – 1513Combined sources
Helixi166 – 17611Combined sources
Turni180 – 1834Combined sources
Beta strandi184 – 1907Combined sources
Beta strandi195 – 1995Combined sources
Helixi200 – 2045Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi230 – 23910Combined sources
Helixi242 – 2443Combined sources
Helixi247 – 2504Combined sources
Beta strandi251 – 2566Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi265 – 2684Combined sources
Beta strandi273 – 2786Combined sources
Helixi281 – 2855Combined sources
Beta strandi286 – 2916Combined sources
Helixi292 – 30110Combined sources
Beta strandi306 – 3138Combined sources
Beta strandi323 – 3275Combined sources
Beta strandi335 – 34612Combined sources
Beta strandi351 – 3599Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K28X-ray2.90D1-391[»]
1PDJelectron microscopy12.00D/E/F1-391[»]
1WTHX-ray2.80D1-391[»]
2Z6BX-ray3.11D1-391[»]
ProteinModelPortaliP17172.
SMRiP17172. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17172.

Family & Domainsi

Family and domain databases

InterProiIPR015180. Phage_T4_Gp27_C.
IPR015181. Phage_T4_Gp27_N.
[Graphical view]
PfamiPF09097. Phage-tail_1. 1 hit.
PF09096. Phage-tail_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMLQRPGYP NLSVKLFDSY DAWSNNRFVE LAATITTLTM RDSLYGRNEG
60 70 80 90 100
MLQFYDSKNI HTKMDGNEII QISVANANDI NNVKTRIYGC KHFSVSVDSK
110 120 130 140 150
GDNIIAIELG TIHSIENLKF GRPFFPDAGE SIKEMLGVIY QDRTLLTPAI
160 170 180 190 200
NAINAYVPDI PWTSTFENYL SYVREVALAV GSDKFVFVWQ DIMGVNMMDY
210 220 230 240 250
DMMINQEPYP MIVGEPSLIG QFIQELKYPL AYDFVWLTKS NPHKRDPMKN
260 270 280 290 300
ATIYAHSFLD SSIPMITTGK GENSIVVSRS GAYSEMTYRN GYEEAIRLQT
310 320 330 340 350
MAQYDGYAKC STIGNFNLTP GVKIIFNDSK NQFKTEFYVD EVIHELSNNN
360 370 380 390
SVTHLYMFTN ATKLETIDPV KVKNEFKSDT TTEESSSSNK Q
Length:391
Mass (Da):44,389
Last modified:December 19, 2001 - v4
Checksum:i0DABEFE1D890B1FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681N → T in CAA36481 (PubMed:2349100).Curated
Sequence conflicti262 – 2621S → E (PubMed:2349100).Curated
Sequence conflicti308 – 3081A → L in CAA36481 (PubMed:2349100).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52236 Genomic DNA. Translation: CAA36481.1.
AF158101 Genomic DNA. Translation: AAD42435.2.
J04354 Genomic DNA. Translation: AAA88466.1.
PIRiJU0285. GZBPT4.
RefSeqiNP_049803.1. NC_000866.4.

Genome annotation databases

GeneIDi1258643.
KEGGivg:1258643.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52236 Genomic DNA. Translation: CAA36481.1.
AF158101 Genomic DNA. Translation: AAD42435.2.
J04354 Genomic DNA. Translation: AAA88466.1.
PIRiJU0285. GZBPT4.
RefSeqiNP_049803.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K28X-ray2.90D1-391[»]
1PDJelectron microscopy12.00D/E/F1-391[»]
1WTHX-ray2.80D1-391[»]
2Z6BX-ray3.11D1-391[»]
ProteinModelPortaliP17172.
SMRiP17172. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17172. 1 interaction.
MINTiMINT-231925.

Protein family/group databases

TCDBi1.K.1.1.1. the gp27/5 t4-baseplate (t4-bp) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258643.
KEGGivg:1258643.

Miscellaneous databases

EvolutionaryTraceiP17172.

Family and domain databases

InterProiIPR015180. Phage_T4_Gp27_C.
IPR015181. Phage_T4_Gp27_N.
[Graphical view]
PfamiPF09097. Phage-tail_1. 1 hit.
PF09096. Phage-tail_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Bacteriophage T4 late gene expression: overlapping promoters direct divergent transcription of the base plate gene cluster."
    Scarlato V., Storlazzi A., Gargano S., Cascino A.
    Virology 171:475-483(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
    Strain: D.
  4. "Structure of the bacteriophage T4 baseplate as determined by chemical cross-linking."
    Watts N.R., Coombs D.H.
    J. Virol. 64:143-154(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Homotrimeric, beta-stranded viral adhesins and tail proteins."
    Weigele P.R., Scanlon E., King J.
    J. Bacteriol. 185:4022-4030(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GP5, SUBUNIT.
  6. Cited for: REVIEW.
  7. Cited for: REVIEW ON FUNCTION.
  8. "The baseplate wedges of bacteriophage T4 spontaneously assemble into hubless baseplate-like structure in vitro."
    Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.
    J. Mol. Biol. 395:349-360(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT.
  10. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
  11. "Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host."
    Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V., Rossmann M.G.
    Cell 118:419-429(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED TAIL, SUBCELLULAR LOCATION, FUNCTION.
  12. "Control of bacteriophage T4 tail lysozyme activity during the infection process."
    Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., Arisaka F.
    J. Mol. Biol. 346:1013-1020(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiBP27_BPT4
AccessioniPrimary (citable) accession number: P17172
Secondary accession number(s): Q9T0T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 19, 2001
Last modified: May 27, 2015
This is version 88 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.