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Protein

Tail spike protein

Gene
N/A
Organism
Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)
Status
Reviewed-Annotation score: -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.2 Publications1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei248Substrate binding1 Publication1
Sitei294Substrate binding1 Publication1
Active sitei367Shared with dimeric partner1 Publication1
Active sitei400Shared with dimeric partner1 Publication1

GO - Molecular functioni

  • endo-1,3-alpha-L-rhamnosidase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processDegradation 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 spike proteinCurated
Short name:
TSP
Alternative name(s):
Endo-1,3-alpha-L-rhamnosidaseCurated (EC:3.2.1.-3 Publications)
EndorhamnosidaseCurated
OrganismiShigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)
Taxonomic identifieri10761 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeP22virus
Virus hostiShigella flexneri [TaxID: 623]

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Viral tail fiber protein, Viral tail protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi248D → N: 98.5% loss of enzymatic activity. 1 Publication1
Mutagenesisi294E → Q: 87% loss of enzymatic activity. 1 Publication1
Mutagenesisi367E → Q: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi400D → N: Almost complete loss of enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000777581 – 623Tail spike proteinAdd BLAST623

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

DIPiDIP-29798N

Structurei

Secondary structure

1623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9XJP3
SMRiQ9XJP3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XJP3

Family & Domainsi

Domaini

The active site involves residues located on two different subunits.1 Publication

Sequence similaritiesi

Family and domain databases

Gene3Di2.160.20.10, 1 hit
2.170.14.10, 1 hit
InterProiView protein in InterPro
IPR009093 P22_tailspike_N
IPR036730 P22_tailspike_N_sf
IPR024535 Pectate_lyase_SF_prot
IPR012334 Pectin_lyas_fold
IPR011050 Pectin_lyase_fold/virulence
PfamiView protein in Pfam
PF09008 Head_binding, 1 hit
PF12708 Pectate_lyase_3, 1 hit
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

Similar proteinsi

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
PDB 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
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
InterProiView protein in InterPro
IPR009093 P22_tailspike_N
IPR036730 P22_tailspike_N_sf
IPR024535 Pectate_lyase_SF_prot
IPR012334 Pectin_lyas_fold
IPR011050 Pectin_lyase_fold/virulence
PfamiView protein in Pfam
PF09008 Head_binding, 1 hit
PF12708 Pectate_lyase_3, 1 hit
SUPFAMiSSF51126 SSF51126, 1 hit
SSF51327 SSF51327, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFIBER_BPSFV
AccessioniPrimary (citable) accession number: Q9XJP3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 30, 2003
Last modified: October 25, 2017
This is version 73 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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