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Protein

Tail sheath protein

Gene

18

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Structural component of the bacteriophage tail which consists of a contractile sheath, a tube and a baseplate. The central cylindrical segment of the tail consists of a rigid tube, composed of multiple copies of gp19, surrounded by the outer contractile sheath assembled from gp18 subunits. A total of 138 copies of gp18 arranged into 23 hexameric rings constitutes the sheath. During infection, contraction of the sheath drives the central tube through the host outer membrane, creating a channel for DNA ejection from the capsid into the host cell.1 Publication

GO - Biological processi

Keywordsi

Molecular functionViral contractile tail ejection system
Biological process

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Tail sheath protein
Short name:
TSP
Alternative name(s):
Gene product 18
Short name:
gp18
Gene namesi
Name:18
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4virus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000009087 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • virion Source: CACAO
  • virus tail, sheath Source: UniProtKB

Keywords - Cellular componenti

Viral tail protein, Viral tail sheath protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by host
ChainiPRO_00001650072 – 659Tail sheath proteinAdd BLAST658

Interactioni

Subunit structurei

Hexamer.

Structurei

Secondary structure

1659
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 31Combined sources6
Beta strandi42 – 44Combined sources3
Helixi48 – 54Combined sources7
Turni59 – 61Combined sources3
Helixi62 – 69Combined sources8
Turni70 – 74Combined sources5
Beta strandi76 – 82Combined sources7
Turni86 – 88Combined sources3
Beta strandi93 – 95Combined sources3
Beta strandi99 – 105Combined sources7
Beta strandi115 – 120Combined sources6
Beta strandi123 – 134Combined sources12
Beta strandi140 – 144Combined sources5
Helixi148 – 157Combined sources10
Turni160 – 162Combined sources3
Beta strandi167 – 171Combined sources5
Beta strandi181 – 187Combined sources7
Beta strandi198 – 200Combined sources3
Helixi201 – 205Combined sources5
Helixi208 – 217Combined sources10
Beta strandi222 – 226Combined sources5
Helixi229 – 233Combined sources5
Beta strandi234 – 240Combined sources7
Helixi241 – 244Combined sources4
Helixi245 – 249Combined sources5
Beta strandi251 – 255Combined sources5
Beta strandi260 – 262Combined sources3
Helixi265 – 268Combined sources4
Beta strandi278 – 285Combined sources8
Beta strandi288 – 298Combined sources11
Helixi311 – 316Combined sources6
Beta strandi321 – 325Combined sources5
Beta strandi336 – 339Combined sources4
Helixi347 – 349Combined sources3
Helixi352 – 358Combined sources7
Helixi360 – 362Combined sources3
Turni365 – 367Combined sources3
Helixi376 – 378Combined sources3
Helixi383 – 400Combined sources18
Helixi411 – 414Combined sources4
Beta strandi415 – 417Combined sources3
Helixi419 – 429Combined sources11
Beta strandi446 – 449Combined sources4
Beta strandi453 – 459Combined sources7
Turni460 – 463Combined sources4
Beta strandi464 – 470Combined sources7
Helixi471 – 480Combined sources10
Beta strandi505 – 507Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FO8X-ray1.80D83-365[»]
3FOAX-ray3.50A/B/C/D1-510[»]
3FOHelectron microscopy15.00A/B/C/D/E/F1-510[»]
3FOIelectron microscopy16.00A/B/C/D/E/F1-510[»]
3J2Melectron microscopy15.00U/V/W/X/Y/Z1-659[»]
3J2Nelectron microscopy16.00U/V/W/X/Y/Z1-659[»]
SMRiP13332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13332.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi172 – 176Ser-rich5

Sequence similaritiesi

Phylogenomic databases

KOiK21531.
OrthoDBiVOG0900003X.

Family and domain databases

InterProiView protein in InterPro
IPR035326. Phage_sheath_beta.
IPR035089. Phage_sheath_subtilisin.
IPR020287. Tail_sheath_C.
PfamiView protein in Pfam
PF04984. Phage_sheath_1. 1 hit.
PF17482. Phage_sheath_1C. 1 hit.
PF17481. Phage_sheath_1N. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P13332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLLSPGIEL KETTVQSTVV NNSTGTAALA GKFQWGPAFQ IKQVTNEVDL
60 70 80 90 100
VNTFGQPTAE TADYFMSAMN FLQYGNDLRV VRAVDRDTAK NSSPIAGNID
110 120 130 140 150
YTISTPGSNY AVGDKITVKY VSDDIETEGK ITEVDADGKI KKINIPTGKN
160 170 180 190 200
YAKAKEVGEY PTLGSNWTAE ISSSSSGLAA VITLGKIITD SGILLAEIEN
210 220 230 240 250
AEAAMTAVDF QANLKKYGIP GVVALYPGEL GDKIEIEIVS KADYAKGASA
260 270 280 290 300
LLPIYPGGGT RASTAKAVFG YGPQTDSQYA IIVRRNDAIV QSVVLSTKRG
310 320 330 340 350
EKDIYDSNIY IDDFFAKGGS EYIFATAQNW PEGFSGILTL SGGLSSNAEV
360 370 380 390 400
TAGDLMEAWD FFADRESVDV QLFIAGSCAG ESLETASTVQ KHVVSIGDAR
410 420 430 440 450
QDCLVLCSPP RETVVGIPVT RAVDNLVNWR TAAGSYTDNN FNISSTYAAI
460 470 480 490 500
DGNHKYQYDK YNDVNRWVPL AADIAGLCAR TDNVSQTWMS PAGYNRGQIL
510 520 530 540 550
NVIKLAIETR QAQRDRLYQE AINPVTGTGG DGYVLYGDKT ATSVPSPFDR
560 570 580 590 600
INVRRLFNML KTNIGRSSKY RLFELNNAFT RSSFRTETAQ YLQGNKALGG
610 620 630 640 650
IYEYRVVCDT TNNTPSVIDR NEFVATFYIQ PARSINYITL NFVATATGAD

FDELTGLAG
Length:659
Mass (Da):71,331
Last modified:January 23, 2007 - v5
Checksum:i5E5974F5BF799816
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti100D → E in AAA32541 (PubMed:2964531).Curated1
Sequence conflicti148 – 151GKNY → AKII in AAA32541 (PubMed:2964531).Curated4
Sequence conflicti301E → G in AAA32541 (PubMed:2964531).Curated1
Sequence conflicti399A → V in AAA32541 (PubMed:2964531).Curated1
Sequence conflicti454H → Y in AAA32541 (PubMed:2964531).Curated1
Sequence conflicti595N → I in AAA32541 (PubMed:2964531).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19085 Genomic DNA. Translation: AAA32541.1.
AF158101 Genomic DNA. Translation: AAD42423.1.
PIRiA60885.
JF0021. GKBPT4.
RefSeqiNP_049780.1. NC_000866.4.

Genome annotation databases

GeneIDi1258597.
KEGGivg:1258597.

Similar proteinsi

Entry informationi

Entry nameiTSP_BPT4
AccessioniPrimary (citable) accession number: P13332
Secondary accession number(s): Q9T0U3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 99 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families