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Protein

Tail fiber protein

Gene

9

Organism
Enterobacteria phage P22 (Bacteriophage P22)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Structural component of the short non-contractile tail. The tail comprises six fibers 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

GO - Molecular functioni

GO - Biological processi

  • entry into host via enzymatic degradation of host anatomical structure Source: UniProtKB
  • 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 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 fiber proteinCurated (EC:3.2.1.-)
Alternative name(s):
Endo-1,3-alpha-L-rhamnosidaseCurated
EndorhamnosidaseCurated
Gene product 9Curated
Short name:
gp9
Tail spike proteinCurated
Short name:
TSP
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

  • 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 – 667667Tail fiber proteinPRO_0000077757Add
BLAST

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

1
667
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 234Combined sources
Beta strandi30 – 356Combined sources
Helixi43 – 453Combined sources
Beta strandi49 – 524Combined sources
Beta strandi58 – 614Combined sources
Beta strandi63 – 675Combined sources
Beta strandi73 – 753Combined sources
Beta strandi82 – 865Combined sources
Beta strandi89 – 935Combined sources
Beta strandi99 – 1046Combined sources
Helixi106 – 1083Combined sources
Helixi114 – 1218Combined sources
Beta strandi125 – 1273Combined sources
Helixi128 – 1303Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 1407Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi177 – 1837Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi203 – 2053Combined sources
Helixi218 – 2225Combined sources
Beta strandi229 – 2335Combined sources
Helixi238 – 2425Combined sources
Turni243 – 2453Combined sources
Helixi246 – 2494Combined sources
Helixi252 – 2543Combined sources
Beta strandi261 – 2677Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi277 – 28711Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi334 – 3418Combined sources
Turni343 – 3464Combined sources
Beta strandi349 – 3524Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi377 – 3793Combined sources
Beta strandi381 – 3899Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi402 – 4043Combined sources
Turni415 – 4173Combined sources
Beta strandi428 – 4358Combined sources
Beta strandi438 – 44811Combined sources
Beta strandi450 – 4589Combined sources
Beta strandi460 – 47011Combined sources
Beta strandi472 – 4809Combined sources
Beta strandi490 – 4934Combined sources
Beta strandi498 – 5047Combined sources
Beta strandi516 – 52914Combined sources
Helixi533 – 5353Combined sources
Beta strandi536 – 5416Combined sources
Beta strandi548 – 5536Combined sources
Beta strandi555 – 5639Combined sources
Turni566 – 5683Combined sources
Beta strandi570 – 5723Combined sources
Beta strandi574 – 5818Combined sources
Beta strandi590 – 5989Combined sources
Beta strandi601 – 61010Combined sources
Helixi611 – 6133Combined sources
Beta strandi616 – 6183Combined sources
Beta strandi622 – 6243Combined sources
Helixi628 – 6303Combined sources
Beta strandi633 – 64210Combined sources
Turni643 – 6464Combined sources
Beta strandi647 – 6537Combined sources
Beta strandi659 – 6657Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-109, 114-667.
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
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. Positions 6-109, 114-667.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH90. Glycoside Hydrolase Family 90.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Phage P22 tail protein: gene and amino acid sequence."
    Sauer R.T., Krovatin W., Poteete A.R., Berget P.B.
    Biochemistry 21:5811-5815(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of the genome of Salmonella bacteriophage P22."
    Vander Byl C.S., Kropinski A.M.B.
    J. Bacteriol. 182:6472-6481(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Homotrimeric, beta-stranded viral adhesins and tail proteins."
    Weigele P.R., Scanlon E., King J.
    J. Bacteriol. 185:4022-4030(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro."
    Andres D., Hanke C., Baxa U., Seul A., Barbirz S., Seckler R.
    J. Biol. Chem. 285:36768-36775(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST LIPOPOLYSACCHARIDES.
  6. "Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer."
    Steinbacher S., Seckler R., Miller S., Steipe B., Huber R., Reinemer P.
    Science 265:383-386(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 110-667.
  7. "Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors."
    Steinbacher S., Baxa U., Miller S., Weintraub A., Seckler R., Huber R.
    Proc. Natl. Acad. Sci. U.S.A. 93:10584-10588(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 110-667 IN COMPLEX WITH O-ANTIGEN.
  8. "Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56-A resolution, and the molecular basis of O-antigen recognition and cleavage."
    Steinbacher S., Miller S., Baxa U., Budisa N., Weintraub A., Seckler R., Huber R.
    J. Mol. Biol. 267:865-880(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 6-109.
  9. "Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity."
    Baxa U., Steinbacher S., Weintraub A., Huber R., Seckler R.
    J. Mol. Biol. 293:693-701(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 114-667.
  10. "Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein."
    Schuler B., Furst F., Osterroth F., Steinbacher S., Huber R., Seckler R.
    Proteins 39:89-101(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 109-667.

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: June 8, 2016
This is version 118 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.