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Protein

Fibritin

Gene

wac

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

Functioni

Chaperone responsible for attachment of long tail fibers to virus particle. During phage assembly, twelve fibritin molecules attach to the phage neck via gp13: six molecules forming the collar and six molecules forming the whiskers.2 Publications

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Fibritin
Alternative name(s):
Collar protein
Whisker antigen control protein
Gene namesi
Name:wac
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 tail fiber protein, Viral tail protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host
Chaini2 – 487486FibritinPRO_0000165075Add
BLAST

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homotrimer (PubMed:9261070, PubMed:15033360, PubMed:19361528). Interacts (via N-terminal domain) with neck protein gp13; this interaction allows attachment of the fibrous collar and wiskers PubMed:23434847.4 Publications

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156Combined sources
Beta strandi36 – 394Combined sources
Turni44 – 463Combined sources
Helixi47 – 8135Combined sources
Helixi373 – 38614Combined sources
Beta strandi389 – 3924Combined sources
Helixi393 – 40513Combined sources
Helixi414 – 4174Combined sources
Helixi422 – 45635Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi470 – 4734Combined sources
Beta strandi476 – 4794Combined sources
Helixi480 – 4834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA0X-ray2.20A372-484[»]
1AVYX-ray1.85A/B/C414-487[»]
1OX3X-ray2.00A2-81[»]
1RFONMR-A/B/C458-484[»]
1V1HX-ray1.90A/B/C/D/E/F456-484[»]
1V1IX-ray1.90A/B/C456-484[»]
2BSGelectron microscopy15.00A/B/C1-487[»]
2IBLX-ray1.32A2-81[»]
2KBLNMR-A458-484[»]
3A1MX-ray2.00A/B/C/D/E/F458-484[»]
3J2Oelectron microscopy25.00A/B/C/D/E/F2-487[»]
4MMQX-ray3.25B458-484[»]
4MMRX-ray3.10B458-484[»]
4MMSX-ray2.40B/D/F458-484[»]
4MMTX-ray3.05B458-484[»]
4MMUX-ray3.00B458-484[»]
4MMVX-ray2.81B458-484[»]
4NCUX-ray1.11A458-484[»]
4NCVX-ray1.20A/B/C458-484[»]
4NCWX-ray1.30A/B/C458-484[»]
ProteinModelPortaliP10104.
SMRiP10104. Positions 3-81, 372-484.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10104.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili52 – 84332 PublicationsAdd
BLAST
Coiled coili99 – 131332 PublicationsAdd
BLAST
Coiled coili145 – 156122 PublicationsAdd
BLAST
Coiled coili177 – 195192 PublicationsAdd
BLAST
Coiled coili210 – 221122 PublicationsAdd
BLAST
Coiled coili232 – 257262 PublicationsAdd
BLAST
Coiled coili265 – 284202 PublicationsAdd
BLAST
Coiled coili289 – 300122 PublicationsAdd
BLAST
Coiled coili309 – 327192 PublicationsAdd
BLAST
Coiled coili335 – 346122 PublicationsAdd
BLAST
Coiled coili361 – 386262 PublicationsAdd
BLAST
Coiled coili393 – 404122 PublicationsAdd
BLAST
Coiled coili419 – 45436Sequence Analysis2 PublicationsAdd
BLAST

Domaini

The central domain consists of 12 alpha-helical domains (19-40 residues long) with coiled-coil structural patterns.

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di1.20.5.320. 2 hits.
InterProiIPR012284. 6PGD_dom_3.
IPR012473. Fibritin_C.
[Graphical view]
PfamiPF07921. Fibritin_C. 1 hit.
[Graphical view]
PRINTSiPR01880. FIBRITIN.

Sequencei

Sequence statusi: Complete.

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

P10104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDIVLNDLP FVDGPPAEGQ SRISWIKNGE EILGADTQYG SEGSMNRPTV
60 70 80 90 100
SVLRNVEVLD KNIGILKTSL ETANSDIKTI QGILDVSGDI EALAQIGINK
110 120 130 140 150
KDISDLKTLT SEHTEILNGT NNTVDSILAD IGPFNAEANS VYRTIRNDLL
160 170 180 190 200
WIKRELGQYT GQDINGLPVV GNPSSGMKHR IINNTDVITS QGIRLSELET
210 220 230 240 250
KFIESDVGSL TIEVGNLREE LGPKPPSFSQ NVYSRLNEID TKQTTVESDI
260 270 280 290 300
SAIKTSIGYP GNNSIITSVN TNTDNIASIN LELNQSGGIK QRLTVIETSI
310 320 330 340 350
GSDDIPSSIK GQIKDNTTSI ESLNGIVGEN TSSGLRANVS WLNQIVGTDS
360 370 380 390 400
SGGQPSPPGS LLNRVSTIET SVSGLNNAVQ NLQVEIGNNS AGIKGQVVAL
410 420 430 440 450
NTLVNGTNPN GSTVEERGLT NSIKANETNI ASVTQEVNTA KGNISSLQGD
460 470 480
VQALQEAGYI PEAPRDGQAY VRKDGEWVFL STFLSPA
Length:487
Mass (Da):51,872
Last modified:January 23, 2007 - v5
Checksum:i253A30F0F0ED13B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581P → H in CAA31379 (PubMed:12626685).Curated
Sequence conflicti479 – 4791F → L in CAA31379 (PubMed:12626685).Curated
Sequence conflicti481 – 4811S → P (PubMed:3194206).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12888 Genomic DNA. Translation: CAA31379.1.
AF158101 Genomic DNA. Translation: AAD42679.1.
X14868 Genomic DNA. Translation: CAA33006.1.
X06792 Genomic DNA. Translation: CAA29952.1.
PIRiS01917. FIBPT4.
RefSeqiNP_049771.1. NC_000866.4.

Genome annotation databases

GeneIDi1258630.
KEGGivg:1258630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12888 Genomic DNA. Translation: CAA31379.1.
AF158101 Genomic DNA. Translation: AAD42679.1.
X14868 Genomic DNA. Translation: CAA33006.1.
X06792 Genomic DNA. Translation: CAA29952.1.
PIRiS01917. FIBPT4.
RefSeqiNP_049771.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA0X-ray2.20A372-484[»]
1AVYX-ray1.85A/B/C414-487[»]
1OX3X-ray2.00A2-81[»]
1RFONMR-A/B/C458-484[»]
1V1HX-ray1.90A/B/C/D/E/F456-484[»]
1V1IX-ray1.90A/B/C456-484[»]
2BSGelectron microscopy15.00A/B/C1-487[»]
2IBLX-ray1.32A2-81[»]
2KBLNMR-A458-484[»]
3A1MX-ray2.00A/B/C/D/E/F458-484[»]
3J2Oelectron microscopy25.00A/B/C/D/E/F2-487[»]
4MMQX-ray3.25B458-484[»]
4MMRX-ray3.10B458-484[»]
4MMSX-ray2.40B/D/F458-484[»]
4MMTX-ray3.05B458-484[»]
4MMUX-ray3.00B458-484[»]
4MMVX-ray2.81B458-484[»]
4NCUX-ray1.11A458-484[»]
4NCVX-ray1.20A/B/C458-484[»]
4NCWX-ray1.30A/B/C458-484[»]
ProteinModelPortaliP10104.
SMRiP10104. Positions 3-81, 372-484.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258630.
KEGGivg:1258630.

Miscellaneous databases

EvolutionaryTraceiP10104.

Family and domain databases

Gene3Di1.20.5.320. 2 hits.
InterProiIPR012284. 6PGD_dom_3.
IPR012473. Fibritin_C.
[Graphical view]
PfamiPF07921. Fibritin_C. 1 hit.
[Graphical view]
PRINTSiPR01880. FIBRITIN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequence of bacteriophage T4 gene wac."
    Prilipov A.G., Selivanov N.A., Nikolaeva L.I., Mesyanzhinov V.V.
    Nucleic Acids Res. 16:10361-10361(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D.
  2. "Fibritin encoded by bacteriophage T4 gene wac has a parallel triple-stranded alpha-helical coiled-coil structure."
    Efimov V.P., Nepluev I.V., Sobolev B.N., Zurabishvili T.G., Schulthess T., Lustig A., Engel J., Haener M., Aebi U., Venyaminov S.Y., Potekhin S.A., Mesyanzhinov V.V.
    J. Mol. Biol. 242:470-486(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D.
  3. Mesyanzhinov V.V.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 358 AND 479.
    Strain: D.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Nucleotide sequences of bacteriophage T4 genes 13, 14 and 15."
    Selivanov N.A., Prilipov A.G., Mesyanzhinov V.V.
    Nucleic Acids Res. 17:3583-3583(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 480-487.
    Strain: D.
  6. "Nucleotide and deduced amino acid sequence of bacteriophage T4 gene 12."
    Selivanov N.A., Prilipov A.G., Mesyanzhinov V.V.
    Nucleic Acids Res. 16:2334-2334(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
    Strain: D.
  7. "The wac gene product of bacteriophage T4 contains coiled-coil structural patterns."
    Sobolev B.N., Mesyanzhinov V.V.
    J. Biomol. Struct. Dyn. 8:953-965(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, COILED COIL.
  8. "gpwac of the T4-type bacteriophages: structure, function, and evolution of a segmented coiled-coil protein that controls viral infectivity."
    Letarov A., Manival X., Desplats C., Krisch H.M.
    J. Bacteriol. 187:1055-1066(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COILED COIL.
  9. "Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain."
    Tao Y., Strelkov S.V., Mesyanzhinov V.V., Rossmann M.G.
    Structure 5:789-798(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 369-487, COILED COIL, SUBUNIT.
  10. "Structure of bacteriophage T4 fibritin M: a troublesome packing arrangement."
    Strelkov S.V., Tao Y., Shneider M.M., Mesyanzhinov V.V., Rossmann M.G.
    Acta Crystallogr. D 54:805-816(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 414-487.
  11. "Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin."
    Guthe S., Kapinos L., Moglich A., Meier S., Grzesiek S., Kiefhaber T.
    J. Mol. Biol. 337:905-915(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 458-484, SUBUNIT.
  12. "Design and crystal structure of bacteriophage T4 mini-fibritin NCCF."
    Boudko S.P., Strelkov S.V., Engel J., Stetefeld J.
    J. Mol. Biol. 339:927-935(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-81.
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (15.00 ANGSTROMS).
  14. "NMR structure of a monomeric intermediate on the evolutionarily optimized assembly pathway of a small trimerization domain."
    Habazettl J., Reiner A., Kiefhaber T.
    J. Mol. Biol. 389:103-114(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 458-484, SUBUNIT.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (25.00 ANGSTROMS) OF 2-487, INTERACTION WITH GP13, FUNCTION, SUBCELLULAR LOCATION.
  16. "Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer."
    Berthelmann A., Lach J., Grawert M.A., Groll M., Eichler J.
    Org. Biomol. Chem. 12:2606-2614(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 458-484.

Entry informationi

Entry nameiWAC_BPT4
AccessioniPrimary (citable) accession number: P10104
Secondary accession number(s): O10628, Q9T0U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 98 of the entry and version 5 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.