Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tail fiber protein

Gene
N/A
Organism
Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Degradation of host cell envelope components during virus entry, Degradation of host lipopolysaccharides during virus entry, Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Tail fiber proteinCurated (EC:3.2.1.-)
Alternative name(s):
Endo-1,3-alpha-L-rhamnosidaseCurated
EndorhamnosidaseCurated
Tail spike proteinCurated
Short name:
TSP
OrganismiShigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)
Taxonomic identifieri10761 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeP22likevirus
Virus hostiShigella flexneri [TaxID: 623]

Subcellular locationi

GO - Cellular componenti

  • virion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Viral tail fiber protein, Viral tail protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623Tail fiber proteinPRO_0000077758Add
BLAST

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

DIPiDIP-29798N.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi114 – 12310Combined sources
Helixi126 – 1283Combined sources
Helixi135 – 1384Combined sources
Beta strandi139 – 1413Combined sources
Helixi153 – 1575Combined sources
Helixi163 – 1664Combined sources
Beta strandi171 – 1744Combined sources
Helixi177 – 18812Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi207 – 2115Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi228 – 2325Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi263 – 2719Combined sources
Beta strandi282 – 2898Combined sources
Beta strandi291 – 31121Combined sources
Beta strandi313 – 32513Combined sources
Beta strandi328 – 3347Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi348 – 3536Combined sources
Turni358 – 3603Combined sources
Beta strandi367 – 37913Combined sources
Beta strandi381 – 3877Combined sources
Beta strandi390 – 41021Combined sources
Beta strandi413 – 42513Combined sources
Beta strandi434 – 4385Combined sources
Beta strandi448 – 4569Combined sources
Beta strandi467 – 4715Combined sources
Beta strandi478 – 4825Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi501 – 5055Combined sources
Beta strandi507 – 5104Combined sources
Beta strandi512 – 5165Combined sources
Beta strandi520 – 5245Combined sources
Beta strandi526 – 5283Combined sources
Beta strandi530 – 5345Combined sources
Beta strandi542 – 5454Combined sources
Beta strandi547 – 5504Combined sources
Beta strandi553 – 5586Combined sources
Beta strandi565 – 5706Combined sources
Beta strandi579 – 5835Combined sources
Helixi588 – 5903Combined sources
Beta strandi594 – 5985Combined sources
Beta strandi601 – 6055Combined sources
Beta strandi616 – 6227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VBEX-ray1.98A110-623[»]
2VBKX-ray1.25A110-623[»]
2VBMX-ray2.00A110-623[»]
4URRX-ray1.95A/B/C/D/E/F110-623[»]
ProteinModelPortaliQ9XJP3.
SMRiQ9XJP3. Positions 7-109, 113-623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XJP3.

Family & Domainsi

Domaini

The interdigitation of the polypeptide chains at the C-termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein.By similarity

Sequence similaritiesi

To phage P22 tsp and to phage APSE-1 p36.Curated

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
2.170.14.10. 1 hit.
InterProiIPR009093. P22_tailspike_N.
IPR024535. Pectate_lyase_SF_prot.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF09008. Head_binding. 1 hit.
PF12708. Pectate_lyase_3. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
SSF51327. SSF51327. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9XJP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDIITNVVI GMPSQLFTMA RSFKAVANGK IYIGKIDTDP VNPENQIQVY
60 70 80 90 100
VENEDGSHVP ASQPIVINAA GYPVYNGQIV KFVTEQGHSM AVYDAYGSQQ
110 120 130 140 150
FYFQNVLKYD PDQFGPDLIE QLAQSGKYSQ DNTKGDAMIG VKQPLPKAVL
160 170 180 190 200
RTQHDKNKEA ISILDFGVID DGVTDNYQAI QNAIDAVASL PSGGELFIPA
210 220 230 240 250
SNQAVGYIVG STLLIPGGVN IRGVGKASQL RAKSGLTGSV LRLSYDSDTI
260 270 280 290 300
GRYLRNIRVT GNNTCNGIDT NITAEDSVIR QVYGWVFDNV MVNEVETAYL
310 320 330 340 350
MQGLWHSKFI ACQAGTCRVG LHFLGQCVSV SVSSCHFSRG NYSADESFGI
360 370 380 390 400
RIQPQTYAWS SEAVRSEAII LDSETMCIGF KNAVYVHDCL DLHMEQLDLD
410 420 430 440 450
YCGSTGVVIE NVNGGFSFSN SWIAADADGT EQFTGIYFRT PTSTQSHKIV
460 470 480 490 500
SGVHINTANK NTAANNQSIA IEQSAIFVFV SGCTLTGDEW AVNIVDINEC
510 520 530 540 550
VSFDKCIFNK PLRYLRSGGV SVTDCYLAGI TEVQKPEGRY NTYRGCSGVP
560 570 580 590 600
SVNGIINVPV AVGATSGSAA IPNPGNLTYR VRSLFGDPAS SGDKVSVSGV
610 620
TINVTRPSPV GVALPSMVEY LAI
Length:623
Mass (Da):67,066
Last modified:May 30, 2003 - v2
Checksum:i481FA9C23C349A9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128887 Genomic DNA. Translation: AAD33394.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128887 Genomic DNA. Translation: AAD33394.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VBEX-ray1.98A110-623[»]
2VBKX-ray1.25A110-623[»]
2VBMX-ray2.00A110-623[»]
4URRX-ray1.95A/B/C/D/E/F110-623[»]
ProteinModelPortaliQ9XJP3.
SMRiQ9XJP3. Positions 7-109, 113-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29798N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XJP3.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
2.170.14.10. 1 hit.
InterProiIPR009093. P22_tailspike_N.
IPR024535. Pectate_lyase_SF_prot.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF09008. Head_binding. 1 hit.
PF12708. Pectate_lyase_3. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
SSF51327. SSF51327. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The Shigella flexneri bacteriophage Sf6 tailspike protein (TSP)/endorhamnosidase is related to the bacteriophage P22 TSP and has a motif common to exo- and endoglycanases, and C-5 epimerases."
    Chua J.E.H., Manning P.A., Morona R.
    Microbiology 145:1649-1659(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The tailspike protein of Shigella phage Sf6: a structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain."
    Freiberg A., Morona R., Van Den Bosch L., Jung C., Behlke J., Carlin N., Seckler R., Baxa U.
    J. Biol. Chem. 278:1542-1548(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO 240-251, SUBUNIT.

Entry informationi

Entry nameiFIBER_BPSFV
AccessioniPrimary (citable) accession number: Q9XJP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 30, 2003
Last modified: January 20, 2016
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.