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Protein

Tail spike protein

Gene

9

Organism
Enterobacteria phage P22 (Bacteriophage P22)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Structural component of the short non-contractile tail. The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei3601 Publication1
Active sitei3931 Publication1
Active sitei3961 Publication1

GO - Molecular functioni

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

GO - Biological processi

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 adhesion receptor, Viral attachment to host cell, Virus entry into host cell

Protein family/group databases

CAZyiGH90. Glycoside Hydrolase Family 90.

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.-2 Publications)
EndorhamnosidaseCurated
Gene product 9Curated
Short name:
gp9
Gene namesi
Name:9
OrganismiEnterobacteria phage P22 (Bacteriophage P22)
Taxonomic identifieri10754 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeP22likevirus
Virus hostiSalmonella typhimurium [TaxID: 90371]
Proteomesi
  • UP000001795 Componenti: Genome
  • UP000007960 Componenti: Genome

Subcellular locationi

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
Mutagenesisi360E → Q: Complete loss of hydrolysis of O-antigen oligosaccharides. 1 Publication1
Mutagenesisi393D → N: Complete loss of hydrolysis of O-antigen oligosaccharides. 1 Publication1
Mutagenesisi396D → N: Complete loss of hydrolysis of O-antigen oligosaccharides. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000777571 – 667Tail spike proteinAdd BLAST667

Proteomic databases

PRIDEiP12528.

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homotrimer. Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen.2 Publications

Structurei

Secondary structure

1667
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 23Combined sources4
Beta strandi30 – 35Combined sources6
Helixi43 – 45Combined sources3
Beta strandi49 – 52Combined sources4
Beta strandi58 – 61Combined sources4
Beta strandi63 – 67Combined sources5
Beta strandi73 – 75Combined sources3
Beta strandi82 – 86Combined sources5
Beta strandi89 – 93Combined sources5
Beta strandi99 – 104Combined sources6
Helixi106 – 108Combined sources3
Helixi114 – 121Combined sources8
Beta strandi125 – 127Combined sources3
Helixi128 – 130Combined sources3
Beta strandi131 – 133Combined sources3
Helixi134 – 140Combined sources7
Beta strandi142 – 147Combined sources6
Beta strandi158 – 160Combined sources3
Beta strandi167 – 170Combined sources4
Beta strandi172 – 175Combined sources4
Beta strandi177 – 183Combined sources7
Beta strandi190 – 193Combined sources4
Beta strandi195 – 197Combined sources3
Beta strandi203 – 205Combined sources3
Helixi218 – 222Combined sources5
Beta strandi229 – 233Combined sources5
Helixi238 – 242Combined sources5
Turni243 – 245Combined sources3
Helixi246 – 249Combined sources4
Helixi252 – 254Combined sources3
Beta strandi261 – 267Combined sources7
Beta strandi272 – 275Combined sources4
Beta strandi277 – 287Combined sources11
Beta strandi292 – 295Combined sources4
Beta strandi297 – 301Combined sources5
Beta strandi306 – 310Combined sources5
Beta strandi312 – 315Combined sources4
Beta strandi321 – 324Combined sources4
Beta strandi326 – 329Combined sources4
Beta strandi334 – 341Combined sources8
Turni343 – 346Combined sources4
Beta strandi349 – 352Combined sources4
Beta strandi354 – 357Combined sources4
Beta strandi362 – 365Combined sources4
Beta strandi368 – 370Combined sources3
Beta strandi377 – 379Combined sources3
Beta strandi381 – 389Combined sources9
Beta strandi394 – 397Combined sources4
Beta strandi402 – 404Combined sources3
Turni415 – 417Combined sources3
Beta strandi428 – 435Combined sources8
Beta strandi438 – 448Combined sources11
Beta strandi450 – 458Combined sources9
Beta strandi460 – 470Combined sources11
Beta strandi472 – 480Combined sources9
Beta strandi490 – 493Combined sources4
Beta strandi498 – 504Combined sources7
Beta strandi516 – 529Combined sources14
Helixi533 – 535Combined sources3
Beta strandi536 – 541Combined sources6
Beta strandi548 – 553Combined sources6
Beta strandi555 – 563Combined sources9
Turni566 – 568Combined sources3
Beta strandi570 – 572Combined sources3
Beta strandi574 – 581Combined sources8
Beta strandi590 – 598Combined sources9
Beta strandi601 – 610Combined sources10
Helixi611 – 613Combined sources3
Beta strandi616 – 618Combined sources3
Beta strandi622 – 624Combined sources3
Helixi628 – 630Combined sources3
Beta strandi633 – 642Combined sources10
Turni643 – 646Combined sources4
Beta strandi647 – 653Combined sources7
Beta strandi659 – 665Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLWX-ray2.00A114-667[»]
1LKTX-ray2.60A/B/C/D/E/F6-109[»]
1QA1X-ray2.00A114-667[»]
1QA2X-ray2.00A114-667[»]
1QA3X-ray2.00A114-667[»]
1QQ1X-ray1.80A109-667[»]
1QRBX-ray2.00A109-667[»]
1QRCX-ray2.50A109-667[»]
1TSPX-ray2.00A109-667[»]
1TYUX-ray1.80A114-667[»]
1TYVX-ray1.80A114-667[»]
1TYWX-ray1.80A114-667[»]
1TYXX-ray1.80A114-667[»]
2VFMX-ray1.50A110-667[»]
2VFNX-ray1.50A110-667[»]
2VFOX-ray1.50A110-667[»]
2VFPX-ray1.55A110-667[»]
2VFQX-ray1.55A110-667[»]
2VKYX-ray2.05B2-124[»]
2VNLX-ray1.80A2-122[»]
2XC1X-ray1.65A/B/C2-667[»]
3TH0X-ray1.75A109-667[»]
5GAIelectron microscopy10.500/Y/Z6-667[»]
ProteinModelPortaliP12528.
SMRiP12528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12528.

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.

Sequence similaritiesi

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.170.14.10. 1 hit.
InterProiIPR015331. P22_tailspike_C.
IPR012332. P22_tailspike_C-like.
IPR009093. P22_tailspike_N.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF09008. Head_binding. 1 hit.
PF09251. PhageP22-tail. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
SSF51327. SSF51327. 1 hit.

Sequencei

Sequence statusi: Complete.

P12528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDITANVVV SNPRPIFTES RSFKAVANGK IYIGQIDTDP VNPANQIPVY
60 70 80 90 100
IENEDGSHVQ ITQPLIINAA GKIVYNGQLV KIVTVQGHSM AIYDANGSQV
110 120 130 140 150
DYIANVLKYD PDQYSIEADK KFKYSVKLSD YPTLQDAASA AVDGLLIDRD
160 170 180 190 200
YNFYGGETVD FGGKVLTIEC KAKFIGDGNL IFTKLGKGSR IAGVFMESTT
210 220 230 240 250
TPWVIKPWTD DNQWLTDAAA VVATLKQSKT DGYQPTVSDY VKFPGIETLL
260 270 280 290 300
PPNAKGQNIT STLEIRECIG VEVHRASGLM AGFLFRGCHF CKMVDANNPS
310 320 330 340 350
GGKDGIITFE NLSGDWGKGN YVIGGRTSYG SVSSAQFLRN NGGFERDGGV
360 370 380 390 400
IGFTSYRAGE SGVKTWQGTV GSTTSRNYNL QFRDSVVIYP VWDGFDLGAD
410 420 430 440 450
TDMNPELDRP GDYPITQYPL HQLPLNHLID NLLVRGALGV GFGMDGKGMY
460 470 480 490 500
VSNITVEDCA GSGAYLLTHE SVFTNIAIID TNTKDFQANQ IYISGACRVN
510 520 530 540 550
GLRLIGIRST DGQGLTIDAP NSTVSGITGM VDPSRINVAN LAEEGLGNIR
560 570 580 590 600
ANSFGYDSAA IKLRIHKLSK TLDSGALYSH INGGAGSGSA YTQLTAISGS
610 620 630 640 650
TPDAVSLKVN HKDCRGAEIP FVPDIASDDF IKDSSCFLPY WENNSTSLKA
660
LVKKPNGELV RLTLATL
Length:667
Mass (Da):71,857
Last modified:October 1, 1989 - v1
Checksum:iD05076D2732A4F7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02473 Genomic DNA. No translation available.
AF217253 Genomic DNA. Translation: AAF75060.1.
BK000583 Genomic DNA. Translation: DAA00981.1.
PIRiA18750. TLBP22.
RefSeqiNP_059644.1. NC_002371.2.

Genome annotation databases

GeneIDi1262799.
KEGGivg:1262799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02473 Genomic DNA. No translation available.
AF217253 Genomic DNA. Translation: AAF75060.1.
BK000583 Genomic DNA. Translation: DAA00981.1.
PIRiA18750. TLBP22.
RefSeqiNP_059644.1. NC_002371.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLWX-ray2.00A114-667[»]
1LKTX-ray2.60A/B/C/D/E/F6-109[»]
1QA1X-ray2.00A114-667[»]
1QA2X-ray2.00A114-667[»]
1QA3X-ray2.00A114-667[»]
1QQ1X-ray1.80A109-667[»]
1QRBX-ray2.00A109-667[»]
1QRCX-ray2.50A109-667[»]
1TSPX-ray2.00A109-667[»]
1TYUX-ray1.80A114-667[»]
1TYVX-ray1.80A114-667[»]
1TYWX-ray1.80A114-667[»]
1TYXX-ray1.80A114-667[»]
2VFMX-ray1.50A110-667[»]
2VFNX-ray1.50A110-667[»]
2VFOX-ray1.50A110-667[»]
2VFPX-ray1.55A110-667[»]
2VFQX-ray1.55A110-667[»]
2VKYX-ray2.05B2-124[»]
2VNLX-ray1.80A2-122[»]
2XC1X-ray1.65A/B/C2-667[»]
3TH0X-ray1.75A109-667[»]
5GAIelectron microscopy10.500/Y/Z6-667[»]
ProteinModelPortaliP12528.
SMRiP12528.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH90. Glycoside Hydrolase Family 90.

Proteomic databases

PRIDEiP12528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1262799.
KEGGivg:1262799.

Miscellaneous databases

EvolutionaryTraceiP12528.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.170.14.10. 1 hit.
InterProiIPR015331. P22_tailspike_C.
IPR012332. P22_tailspike_C-like.
IPR009093. P22_tailspike_N.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF09008. Head_binding. 1 hit.
PF09251. PhageP22-tail. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
SSF51327. SSF51327. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFIBER_BPP22
AccessioniPrimary (citable) accession number: P12528
Secondary accession number(s): Q7PCJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 30, 2016
This is version 122 of the entry and version 1 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. 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.