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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: Annotation score: 5 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.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

  • entry into host via enzymatic degradation of host anatomical structure Source: UniProtKB
  • metabolic process Source: UniProtKB-KW
  • pathogenesis Source: InterPro
  • viral entry into host cell Source: UniProtKB-KW
  • virion attachment to host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, 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 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 stageCaudoviralesPodoviridaeP22likevirus
Virus hostiShigella flexneri [TaxID: 623]

Subcellular locationi

  • Virion 1 Publication

GO - Cellular componenti

  • virus tail, fiber Source: UniProtKB
Complete GO annotation...

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi114 – 123Combined sources10
Helixi126 – 128Combined sources3
Helixi135 – 138Combined sources4
Beta strandi139 – 141Combined sources3
Helixi153 – 157Combined sources5
Helixi163 – 166Combined sources4
Beta strandi171 – 174Combined sources4
Helixi177 – 188Combined sources12
Beta strandi194 – 197Combined sources4
Beta strandi207 – 211Combined sources5
Beta strandi213 – 215Combined sources3
Beta strandi219 – 222Combined sources4
Beta strandi228 – 232Combined sources5
Beta strandi238 – 243Combined sources6
Beta strandi252 – 256Combined sources5
Beta strandi258 – 260Combined sources3
Beta strandi263 – 271Combined sources9
Beta strandi282 – 289Combined sources8
Beta strandi291 – 311Combined sources21
Beta strandi313 – 325Combined sources13
Beta strandi328 – 334Combined sources7
Beta strandi336 – 338Combined sources3
Beta strandi348 – 353Combined sources6
Turni358 – 360Combined sources3
Beta strandi367 – 379Combined sources13
Beta strandi381 – 387Combined sources7
Beta strandi390 – 410Combined sources21
Beta strandi413 – 425Combined sources13
Beta strandi434 – 438Combined sources5
Beta strandi448 – 456Combined sources9
Beta strandi467 – 471Combined sources5
Beta strandi478 – 482Combined sources5
Beta strandi487 – 489Combined sources3
Beta strandi491 – 496Combined sources6
Beta strandi501 – 505Combined sources5
Beta strandi507 – 510Combined sources4
Beta strandi512 – 516Combined sources5
Beta strandi520 – 524Combined sources5
Beta strandi526 – 528Combined sources3
Beta strandi530 – 534Combined sources5
Beta strandi542 – 545Combined sources4
Beta strandi547 – 550Combined sources4
Beta strandi553 – 558Combined sources6
Beta strandi565 – 570Combined sources6
Beta strandi579 – 583Combined sources5
Helixi588 – 590Combined sources3
Beta strandi594 – 598Combined sources5
Beta strandi601 – 605Combined sources5
Beta strandi616 – 622Combined sources7

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...

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.
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
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.
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...

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: November 30, 2016
This is version 70 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
  3. SIMILARITY comments
    Index of protein domains and families

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.