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Protein

Tail spike protein

Gene

9

Organism
Salmonella phage P22 (Bacteriophage P22)
Status
Reviewed-Annotation score: -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

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

Protein family/group databases

CAZyiGH90 Glycoside Hydrolase Family 90
UniLectiniP12528

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
OrganismiSalmonella phage P22 (Bacteriophage P22)
Taxonomic identifieri10754 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeP22virus
Virus hostiSalmonella typhimurium [TaxID: 90371]
Proteomesi
  • UP000001795 Componenti: Genome
  • UP000007960 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

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

Chemistry databases

DrugBankiDB02590 Abequose
DB02379 Beta-D-Glucose
DB04028 Tyvelose

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

3D structure databases

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

Phylogenomic databases

OrthoDBiVOG09000035

Family and domain databases

Gene3Di2.160.20.20, 1 hit
2.170.14.10, 1 hit
InterProiView protein in InterPro
IPR012332 P22_tailspike-like_C_sf
IPR015331 P22_tailspike_C
IPR009093 P22_tailspike_N
IPR036730 P22_tailspike_N_sf
IPR011050 Pectin_lyase_fold/virulence
PfamiView protein in Pfam
PF09008 Head_binding, 1 hit
PF09251 PhageP22-tail, 1 hit
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

Similar proteinsi

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...

Chemistry databases

DrugBankiDB02590 Abequose
DB02379 Beta-D-Glucose
DB04028 Tyvelose

Protein family/group databases

CAZyiGH90 Glycoside Hydrolase Family 90
UniLectiniP12528

Proteomic databases

PRIDEiP12528

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1262799
KEGGivg:1262799

Phylogenomic databases

OrthoDBiVOG09000035

Miscellaneous databases

EvolutionaryTraceiP12528

Family and domain databases

Gene3Di2.160.20.20, 1 hit
2.170.14.10, 1 hit
InterProiView protein in InterPro
IPR012332 P22_tailspike-like_C_sf
IPR015331 P22_tailspike_C
IPR009093 P22_tailspike_N
IPR036730 P22_tailspike_N_sf
IPR011050 Pectin_lyase_fold/virulence
PfamiView protein in Pfam
PF09008 Head_binding, 1 hit
PF09251 PhageP22-tail, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 18, 2018
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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