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Protein

Tail tube protein

Gene

V

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

Functioni

Forms the phage's tail tube composed of 32 hexameric disks. When it encounters the appropriate initiation complex gpM and gpL, it assembles in hexameric rings that stack on top of each others. Multimerization ceases when the correct tail length is achieved through a mechanism dependent on tail terminator protein.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Viral tail assembly, Virus exit from host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Tail tube protein
Short name:
TTP
Alternative name(s):
Gene product V
Short name:
gpV
Major tail protein V
Gene namesi
Name:V
Ordered Locus Names:lambdap13
OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
Taxonomic identifieri10710 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000001711 Componenti: Genome

Subcellular locationi

  • Virion 1 Publication
  • Host cytoplasm 1 Publication

GO - Cellular componenti

  • host cell cytoplasm Source: UniProtKB-SubCell
  • virus tail, tube Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Viral tail protein, Viral tail tube protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Tail tube proteinPRO_0000077671Add
BLAST

Interactioni

Subunit structurei

Multimerizes into a structure formed by 32 hexameric rings stacked on phage baseplate gpM and gpL. Does not multimerize in solution without the tail initiation complex. Soluble major tail protein interacts with tail assembly protein GT during tail assembly.2 Publications

Protein-protein interaction databases

IntActiP03733. 6 interactions.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 194Combined sources
Beta strandi22 – 287Combined sources
Beta strandi32 – 343Combined sources
Beta strandi37 – 4610Combined sources
Beta strandi67 – 693Combined sources
Beta strandi80 – 867Combined sources
Helixi93 – 10210Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1438Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi178 – 1858Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi228 – 2303Combined sources
Turni231 – 2333Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi240 – 2445Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K4QNMR-A1-153[»]
2L04NMR-A160-246[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03733.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR003343. Big_2.
IPR008962. PapD-like.
IPR032494. Phage_TTP_12.
[Graphical view]
PfamiPF02368. Big_2. 1 hit.
PF16461. Phage_TTP_12. 1 hit.
[Graphical view]
SMARTiSM00635. BID_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVPNPTMPV KGAGTTLWVY KGSGDPYANP LSDVDWSRLA KVKDLTPGEL
60 70 80 90 100
TAESYDDSYL DDEDADWTAT GQGQKSAGDT SFTLAWMPGE QGQQALLAWF
110 120 130 140 150
NEGDTRAYKI RFPNGTVDVF RGWVSSIGKA VTAKEVITRT VKVTNVGRPS
160 170 180 190 200
MAEDRSTVTA ATGMTVTPAS TSVVKGQSTT LTVAFQPEGV TDKSFRAVSA
210 220 230 240
DKTKATVSVS GMTITVNGVA AGKVNIPVVS GNGEFAAVAE ITVTAS
Length:246
Mass (Da):25,810
Last modified:July 21, 1986 - v1
Checksum:i3E9B2124FF2E80CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96545.1.
PIRiD43008. TLBPVL.
RefSeqiNP_040592.1. NC_001416.1.

Genome annotation databases

GeneIDi2703487.
KEGGivg:2703487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96545.1.
PIRiD43008. TLBPVL.
RefSeqiNP_040592.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K4QNMR-A1-153[»]
2L04NMR-A160-246[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03733. 6 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703487.
KEGGivg:2703487.

Miscellaneous databases

EvolutionaryTraceiP03733.

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR003343. Big_2.
IPR008962. PapD-like.
IPR032494. Phage_TTP_12.
[Graphical view]
PfamiPF02368. Big_2. 1 hit.
PF16461. Phage_TTP_12. 1 hit.
[Graphical view]
SMARTiSM00635. BID_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Purification and characterization of the major protein and the terminator protein of the bacteriophage lambda tail."
    Katsura I., Tsugita A.
    Virology 76:129-145(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBUNIT, SUBCELLULAR LOCATION.
  3. "Mechanism of length determination in bacteriophage lambda tails."
    Katsura I.
    Adv. Biophys. 26:1-18(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Chaperone-protein interactions that mediate assembly of the bacteriophage lambda tail to the correct length."
    Xu J., Hendrix R.W., Duda R.L.
    J. Mol. Biol. 426:1004-1018(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GPGT.
  5. "The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system."
    Pell L.G., Kanelis V., Donaldson L.W., Howell P.L., Davidson A.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:4160-4165(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-153.
  6. "The solution structure of the C-terminal Ig-like domain of the bacteriophage lambda tail tube protein."
    Pell L.G., Gasmi-Seabrook G.M., Morais M., Neudecker P., Kanelis V., Bona D., Donaldson L.W., Edwards A.M., Howell P.L., Davidson A.R., Maxwell K.L.
    J. Mol. Biol. 403:468-479(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 160-246.

Entry informationi

Entry nameiTUBE_LAMBD
AccessioniPrimary (citable) accession number: P03733
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 72 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, Reference proteome

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.