Tail fiber protein

Details

Name
Tail fiber protein
Synonyms
  • 3.2.1.-
  • Endo-1,3-alpha-L-rhamnosidase
  • Endorhamnosidase
  • Gene product 9
  • gp9
  • Tail spike protein
  • TSP
Gene Name
9
Organism
Enterobacteria phage P22
Amino acid sequence
>lcl|BSEQ0010902|Tail fiber protein
MTDITANVVVSNPRPIFTESRSFKAVANGKIYIGQIDTDPVNPANQIPVYIENEDGSHVQ
ITQPLIINAAGKIVYNGQLVKIVTVQGHSMAIYDANGSQVDYIANVLKYDPDQYSIEADK
KFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNL
IFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDY
VKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPS
GGKDGIITFENLSGDWGKGNYVIGGRTSYGSVSSAQFLRNNGGFERDGGVIGFTSYRAGE
SGVKTWQGTVGSTTSRNYNLQFRDSVVIYPVWDGFDLGADTDMNPELDRPGDYPITQYPL
HQLPLNHLIDNLLVRGALGVGFGMDGKGMYVSNITVEDCAGSGAYLLTHESVFTNIAIID
TNTKDFQANQIYISGACRVNGLRLIGIRSTDGQGLTIDAPNSTVSGITGMVDPSRINVAN
LAEEGLGNIRANSFGYDSAAIKLRIHKLSKTLDSGALYSHINGGAGSGSAYTQLTAISGS
TPDAVSLKVNHKDCRGAEIPFVPDIASDDFIKDSSCFLPYWENNSTSLKALVKKPNGELV
RLTLATL
Number of residues
667
Molecular Weight
71856.28
Theoretical pI
5.25
GO Classification
Functions
hydrolase activity, acting on glycosyl bonds
Processes
pathogenesis / viral entry into host cell / virion attachment to host cell
Components
virion
General Function
Hydrolase activity, acting on glycosyl bonds
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Virion
Gene sequence
>lcl|BSEQ0010903|Tail fiber protein (9)
ATGACAGACATCACTGCAAACGTAGTTGTTTCTAACCCTCGTCCAATCTTCACTGAATCC
CGTTCGTTTAAAGCTGTTGCTAATGGGAAAATTTACATTGGTCAGATTGATACCGATCCG
GTTAATCCTGCCAATCAGATACCCGTATACATTGAAAATGAGGATGGCTCTCACGTCCAG
ATTACTCAGCCGCTAATTATCAACGCAGCCGGTAAAATCGTATACAACGGCCAACTGGTG
AAAATTGTCACCGTTCAGGGTCATAGCATGGCTATCTATGATGCCAATGGTTCTCAGGTT
GACTATATTGCTAACGTATTGAAGTACGATCCAGATCAATATTCAATAGAAGCTGATAAA
AAATTTAAGTATTCAGTAAAATTATCAGATTATCCAACATTGCAGGATGCAGCATCTGCT
GCGGTTGATGGCCTTCTTATCGATCGAGATTATAATTTTTATGGTGGAGAGACAGTTGAT
TTTGGCGGAAAGGTTCTGACTATAGAATGTAAAGCTAAATTTATAGGAGATGGAAATCTT
ATTTTTACGAAATTAGGCAAAGGTTCCCGCATTGCCGGGGTTTTTATGGAAAGCACTACA
ACACCATGGGTTATCAAGCCTTGGACGGATGACAATCAGTGGCTAACGGATGCCGCAGCG
GTCGTTGCCACTTTAAAACAATCTAAAACTGATGGGTATCAGCCAACCGTAAGCGATTAC
GTTAAATTCCCAGGAATAGAAACGTTACTCCCACCTAATGCAAAAGGGCAAAACATAACG
TCTACGTTAGAAATTAGAGAATGTATAGGGGTCGAAGTTCATCGGGCTAGCGGTCTAATG
GCTGGTTTTTTGTTTAGAGGGTGTCACTTCTGCAAGATGGTAGACGCCAATAATCCAAGC
GGAGGTAAAGATGGCATTATAACCTTCGAAAACCTTAGCGGCGATTGGGGGAAGGGTAAC
TATGTCATTGGCGGACGAACCAGCTATGGGTCAGTAAGTAGCGCCCAGTTTTTACGTAAT
AATGGTGGCTTTGAACGTGATGGTGGAGTTATTGGGTTTACTTCATATCGCGCTGGGGAG
AGTGGCGTTAAAACTTGGCAAGGTACTGTGGGCTCGACAACCTCTCGCAACTATAATCTG
CAATTCCGCGACTCGGTCGTTATTTACCCCGTATGGGACGGATTCGATTTAGGTGCTGAC
ACTGACATGAATCCGGAGTTGGACAGGCCAGGGGACTACCCTATAACCCAATACCCACTG
CATCAGTTACCCCTAAATCACCTGATTGATAATCTTCTGGTTCGCGGGGCGTTAGGTGTA
GGTTTTGGTATGGATGGTAAGGGCATGTATGTGTCTAATATTACCGTAGAAGATTGCGCT
GGGTCTGGCGCGTACCTACTCACCCACGAATCAGTATTTACCAATATAGCCATAATTGAC
ACCAATACTAAGGATTTCCAGGCGAATCAGATTTATATATCTGGGGCTTGCCGTGTGAAC
GGTTTACGTTTAATTGGGATCCGCTCAACCGATGGGCAGGGTCTAACCATAGACGCCCCT
AACTCTACCGTAAGCGGTATAACCGGGATGGTAGACCCCTCTAGAATTAATGTTGCTAAT
TTGGCAGAAGAAGGGTTAGGTAATATCCGCGCTAATAGTTTCGGCTATGATAGCGCAGCG
ATTAAACTGCGGATTCATAAGTTATCAAAGACATTAGATAGCGGAGCATTGTACTCCCAC
ATTAACGGGGGGGCCGGTTCTGGCTCAGCGTATACTCAACTTACTGCTATTTCAGGTAGC
ACACCTGACGCTGTATCATTAAAAGTTAACCACAAAGATTGCAGGGGGGCAGAGATACCA
TTTGTTCCTGACATCGCGTCAGATGATTTTATAAAGGATTCCTCATGTTTTTTGCCATAT
TGGGAAAATAATTCTACTTCTTTAAAGGCTTTAGTGAAAAAACCCAATGGAGAATTAGTT
AGATTAACCTTGGCAACACTTTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP12528
UniProtKB Entry NameFIBER_BPP22
GenBank Gene IDJ02473
General References
  1. Sauer RT, Krovatin W, Poteete AR, Berget PB: Phage P22 tail protein: gene and amino acid sequence. Biochemistry. 1982 Nov 9;21(23):5811-5. [Article]
  2. Vander Byl C, Kropinski AM: Sequence of the genome of Salmonella bacteriophage P22. J Bacteriol. 2000 Nov;182(22):6472-81. [Article]
  3. Pedulla ML, Ford ME, Karthikeyan T, Houtz JM, Hendrix RW, Hatfull GF, Poteete AR, Gilcrease EB, Winn-Stapley DA, Casjens SR: Corrected sequence of the bacteriophage p22 genome. J Bacteriol. 2003 Feb;185(4):1475-7. [Article]
  4. Weigele PR, Scanlon E, King J: Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol. 2003 Jul;185(14):4022-30. [Article]
  5. Andres D, Hanke C, Baxa U, Seul A, Barbirz S, Seckler R: Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J Biol Chem. 2010 Nov 19;285(47):36768-75. doi: 10.1074/jbc.M110.169003. Epub 2010 Sep 3. [Article]
  6. Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P: Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science. 1994 Jul 15;265(5170):383-6. [Article]
  7. Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R: Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10584-8. [Article]
  8. Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R: 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. J Mol Biol. 1997 Apr 11;267(4):865-80. [Article]
  9. Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R: Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity. J Mol Biol. 1999 Oct 29;293(3):693-701. [Article]
  10. Schuler B, Furst F, Osterroth F, Steinbacher S, Huber R, Seckler R: Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein. Proteins. 2000 Apr 1;39(1):89-101. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02590AbequoseexperimentalunknownDetails
DB04028TyveloseexperimentalunknownDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails