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P12528 (TSPE_BPP22) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional tail protein
Alternative name(s):
Late protein gp9

Including the following 2 domains:

  1. Tailspike-protein
    Short name=TSP
  2. Endorhamnosidase
    EC=3.2.1.-
    Alternative name(s):
    Endo-1,3-alpha-L-rhamnosidase
Gene names
Name:9
OrganismEnterobacteria phage P22 (Bacteriophage P22)
Taxonomic identifier10754 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › P22-like viruses
Virus hostSalmonella typhimurium [TaxID: 90371]

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5

Subunit structure

Homotrimer. Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen. Ref.5

Subcellular location

Virion Potential.

Domain

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 similarities

To phage SF6 tsp and to phage APSE-1 p36.

Ontologies

Keywords
   Biological processHost-virus interaction
Initiation of viral infection
Viral attachment to host cell
   Cellular componentVirion
   Developmental stageLate protein
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processinterspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular componentvirion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667Bifunctional tail protein
PRO_0000077757

Secondary structure

1 .......................................................................................................................................... 667
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12528 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: D05076D2732A4F7C

FASTA66771,857
        10         20         30         40         50         60 
MTDITANVVV SNPRPIFTES RSFKAVANGK IYIGQIDTDP VNPANQIPVY IENEDGSHVQ 

        70         80         90        100        110        120 
ITQPLIINAA GKIVYNGQLV KIVTVQGHSM AIYDANGSQV DYIANVLKYD PDQYSIEADK 

       130        140        150        160        170        180 
KFKYSVKLSD YPTLQDAASA AVDGLLIDRD YNFYGGETVD FGGKVLTIEC KAKFIGDGNL 

       190        200        210        220        230        240 
IFTKLGKGSR IAGVFMESTT TPWVIKPWTD DNQWLTDAAA VVATLKQSKT DGYQPTVSDY 

       250        260        270        280        290        300 
VKFPGIETLL PPNAKGQNIT STLEIRECIG VEVHRASGLM AGFLFRGCHF CKMVDANNPS 

       310        320        330        340        350        360 
GGKDGIITFE NLSGDWGKGN YVIGGRTSYG SVSSAQFLRN NGGFERDGGV IGFTSYRAGE 

       370        380        390        400        410        420 
SGVKTWQGTV GSTTSRNYNL QFRDSVVIYP VWDGFDLGAD TDMNPELDRP GDYPITQYPL 

       430        440        450        460        470        480 
HQLPLNHLID NLLVRGALGV GFGMDGKGMY VSNITVEDCA GSGAYLLTHE SVFTNIAIID 

       490        500        510        520        530        540 
TNTKDFQANQ IYISGACRVN GLRLIGIRST DGQGLTIDAP NSTVSGITGM VDPSRINVAN 

       550        560        570        580        590        600 
LAEEGLGNIR ANSFGYDSAA IKLRIHKLSK TLDSGALYSH INGGAGSGSA YTQLTAISGS 

       610        620        630        640        650        660 
TPDAVSLKVN HKDCRGAEIP FVPDIASDDF IKDSSCFLPY WENNSTSLKA LVKKPNGELV 


RLTLATL

« Hide

References

« Hide 'large scale' references
[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: 6295443] [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: 11053393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Corrected sequence of the bacteriophage P22 genome."
Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W., Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A., Casjens S.R.
J. Bacteriol. 185:1475-1477(2003) [PubMed: 12562822] [Abstract]
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: 12837775] [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: 20817910] [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: 8023158] [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: 8855221] [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: 9135118] [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: 10543960] [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: 10737931] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 109-667.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02473 Genomic DNA. No translation available.
AF217253 Genomic DNA. Translation: AAF75060.1.
BK000583 Genomic DNA. Translation: DAA00981.1.
PIRTLBP22. A18750.
RefSeqNP_059644.1. NC_002371.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.05B2-123[»]
2VNLX-ray1.80A2-122[»]
2XC1X-ray1.65A/B/C2-667[»]
ProteinModelPortalP12528.
SMRP12528. Positions 6-109, 114-667.
ModBaseSearch...

Protein family/group databases

CAZyGH90. Glycoside Hydrolase Family 90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1262799.
GenomeReviewsGene locus 9 in contig AF217253_GR.
Gene locus 9 in contig BK000583_GR.

Phylogenomic databases

ProtClustDBCLSP2343245.

Family and domain databases

InterProIPR015331. P22_tailspike_C.
IPR012332. P22_tailspike_C-like.
IPR006626. PbH1.
IPR011050. Pectin_lyase_fold/virulence.
IPR009093. Phage_P22_Gp9_tailspike_N.
[Graphical view]
Gene3DG3DSA:2.160.20.20. P22_tailspike. 1 hit.
G3DSA:2.170.14.10. Tailspk_head_bd. 1 hit.
PfamPF09008. Head_binding. 1 hit.
PF09251. PhageP22-tail. 1 hit.
[Graphical view]
SMARTSM00710. PbH1. 2 hits.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF51327. Tailspk_head_bd. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTSPE_BPP22
AccessionPrimary (citable) accession number: P12528
Secondary accession number(s): Q7PCJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents