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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 involved in tail fiber assembly and retraction. Acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. During phage assembly, twelve fibritin molecules attach to the phage neck via gp13: six molecules forming the collar and six molecules forming the whiskers. to assist long.3 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]
Proteomesi
  • UP000009087 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • virion Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Viral tail protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by host
ChainiPRO_00001650752 – 487FibritinAdd BLAST486

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

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 15Combined sources6
Beta strandi36 – 39Combined sources4
Turni44 – 46Combined sources3
Helixi47 – 81Combined sources35
Helixi373 – 386Combined sources14
Beta strandi389 – 392Combined sources4
Helixi393 – 405Combined sources13
Helixi414 – 417Combined sources4
Helixi422 – 456Combined sources35
Beta strandi465 – 467Combined sources3
Beta strandi470 – 473Combined sources4
Beta strandi476 – 479Combined sources4
Helixi480 – 483Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10104.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili52 – 842 PublicationsAdd BLAST33
Coiled coili99 – 1312 PublicationsAdd BLAST33
Coiled coili145 – 1562 PublicationsAdd BLAST12
Coiled coili177 – 1952 PublicationsAdd BLAST19
Coiled coili210 – 2212 PublicationsAdd BLAST12
Coiled coili232 – 2572 PublicationsAdd BLAST26
Coiled coili265 – 2842 PublicationsAdd BLAST20
Coiled coili289 – 3002 PublicationsAdd BLAST12
Coiled coili309 – 3272 PublicationsAdd BLAST19
Coiled coili335 – 3462 PublicationsAdd BLAST12
Coiled coili361 – 3862 PublicationsAdd BLAST26
Coiled coili393 – 4042 PublicationsAdd BLAST12
Coiled coili419 – 454Sequence analysis2 PublicationsAdd BLAST36

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)DescriptionActionsGraphical viewLength
Sequence conflicti358P → H in CAA31379 (PubMed:12626685).Curated1
Sequence conflicti479F → L in CAA31379 (PubMed:12626685).Curated1
Sequence conflicti481S → P (PubMed:3194206).Curated1

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
PDB 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.
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...

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: November 2, 2016
This is version 103 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

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.