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Q858B1 (Q858B1_BPK1F) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names

Endo-alpha-sialidase EMBL CAD44528.2
EC=3.2.1.129 EMBL CAD44528.2

Precursor of gp17 EMBL CAJ29390.1
EC=3.2.1.129 EMBL CAJ29390.1
Gene names
Name:sia EMBL CAD44528.2
Synonyms:17 EMBL CAJ29390.1, 17.0 EMBL AAZ73001.1
OrganismEnterobacteria phage K1F (Bacteriophage K1F) [Complete proteome] EMBL CAD44528.2
Taxonomic identifier344021 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length1064 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Molecular functionGlycosidase EMBL CAD44528.2
Hydrolase
   Technical term3D-structure PDB 1V0E PDB 1V0F
Complete proteome
Gene Ontology (GO)
   Molecular_functionendo-alpha-(2,8)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site8191Phosphate 1; via amide nitrogen PDB 1V0E PDB 1V0F
Binding site8191Phosphate 2; via amide nitrogen PDB 1V0E PDB 1V0F
Binding site8191Phosphate 3; via amide nitrogen PDB 1V0E
Binding site8301Phosphate 1 PDB 1V0E PDB 1V0F
Binding site8301Phosphate 4 PDB 1V0E PDB 1V0F

Sequences

Sequence LengthMass (Da)Tools
Q858B1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 82FAB75EDC68DAB6

FASTA1,064118,905
        10         20         30         40         50         60 
MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF LNPTMIEMLV 

        70         80         90        100        110        120 
DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA IHIAEEGRDQ TVDLAKEYAD 

       130        140        150        160        170        180 
AAGSSAGNAK DSEDEARRIA ESIRAAGLIG YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR 

       190        200        210        220        230        240 
WDGTLPKNVP AGSTPETSGG IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD 

       250        260        270        280        290        300 
ARGWGAKGDG VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP 

       310        320        330        340        350        360 
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH GVSRLHVSWV 

       370        380        390        400        410        420 
KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF AMIETRTLAK NALTNCALWD 

       430        440        450        460        470        480 
RPMSRSLHLT GGITKAANQR YATIHVPDHG LFVGDFVNFS NSAVTGVSGD MTVATVIDKD 

       490        500        510        520        530        540 
NFTVLTPNQQ TSDLNNAGKN WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG 

       550        560        570        580        590        600 
YHQGDVAPRE VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG 

       610        620        630        640        650        660 
DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN EWEAGAPDDR 

       670        680        690        700        710        720 
YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS GVGVGSVVVK DNYIYYMFGG 

       730        740        750        760        770        780 
EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT 

       790        800        810        820        830        840 
NGVRTVPAPM EFTGDLGLGH VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF 

       850        860        870        880        890        900 
CGGEGTSSTT GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT 

       910        920        930        940        950        960 
AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND ARIHFGVIAQ 

       970        980        990       1000       1010       1020 
QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN EIVEHTDEEG NVTTTEEPVY 

      1030       1040       1050       1060 
TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK LERIEARLSA LEQK 

« Hide

References

« Hide 'large scale' references
[1]"Proteolytic processing and oligomerization of bacteriophage-derived endosialidases."
M hlenhoff.M., Stummeyer K., Grove M., Sauerborn M., Gerardy-Schahn R.
J. Biol. Chem. 278:12634-12644(2003)
Cited for: NUCLEOTIDE SEQUENCE OF 2-1064.
[2]"Proteolytic processing and oligomerization of bacteriophage-derived endosialidases."
Muhlenhoff M., Stummeyer K., Grove M., Sauerborn M., Gerardy-Schahn R.
J. Biol. Chem. 278:12634-12644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"The genome of bacteriophage K1F, a T7-like phage that has acquired the ability to replicate on K1 strains of Escherichia coli."
Scholl D., Merril C.
J. Bacteriol. 187:8499-8503(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F."
Stummeyer K., Dickmanns A., Muhlenhoff M., Gerardy-Schahn R., Ficner R.
Nat. Struct. Mol. Biol. 12:90-96(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 246-910 IN COMPLEX WITH PHOSPHATE.
[5]"Endosialidase NF appears to bind polySia DP5 in a helical conformation."
Haselhorst T., Stummeyer K., Muehlenhoff M., Schaper W., Gerardy-Schahn R., von Itzstein M.
ChemBioChem 7:1875-1877(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 2-910.
[6]"Evolution of bacteriophages infecting encapsulated bacteria: lessons from Escherichia coli K1-specific phages."
Stummeyer K.Schwarzer.D., Claus H.Vogel.U., Gerardy-Schahn R.Muhlenhoff., M
Mol. Microbiol. 60:1123-1135(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[7]"Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins."
Schwarzer D., Stummeyer K., Gerardy-Schahn R., and Muehlenhoff M.
J. Biol. Chem. 282:2821-2831(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 2-1064.
[8]"Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F."
Schwarzer D., Stummeyer K., Haselhorst T., Freiberger F., Rode B., Grove M., Scheper T., von Itzstein M., Muehlenhoff M., and Gerardy-Schahn R.
J. Biol. Chem. 284:9465-9474(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 2-1064.
[9]"Structure analysis of endosialidase NF at 0.98 A resolution."
Schulz E.C., Neumann P., Gerardy-Schahn R., Sheldrick G.M., Ficner R.
Acta Crystallogr. D 66:176-180(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 2-910.
[10]"Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF."
Schulz E.C., Schwarzer D., Frank M., Stummeyer K., Muehlenhoff M., Dickmanns A., Gerardy-Schahn R., Ficner R.
J. Mol. Biol. 397:341-351(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 2-910.
[11]"Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding."
Schulz E.C., Dickmanns A., Urlaub H., Schmitt A., Muhlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R.
Nat. Struct. Mol. Biol. 17:210-215(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 790-1064.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ111067 Genomic DNA. Translation: AAZ73001.1.
AJ505988 Genomic DNA. Translation: CAD44528.2.
AM084414 Genomic DNA. Translation: CAJ29390.1.
RefSeqYP_338127.1. NC_007456.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0EX-ray1.90A/B/C/D/E/F246-910[»]
1V0FX-ray2.55A/B/C/D/E/F246-910[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48774N.

Protein family/group databases

CAZyGH58. Glycoside Hydrolase Family 58.
MEROPSS74.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3707741.

Family and domain databases

Gene3D2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProIPR023366. ATPase_asu-like.
IPR024427. Endosialidase_beta_barrel.
IPR024428. Endosialidase_beta_prop.
IPR024430. Endosialidase_C_dom.
IPR024429. Endosialidase_N-extension.
IPR001724. Glycl_Hydrolase_58.
IPR005604. Phage_T7_tail_fibre.
IPR011040. Sialidases.
[Graphical view]
PfamPF12195. End_beta_barrel. 1 hit.
PF12217. End_beta_propel. 1 hit.
PF12218. End_N_terminal. 1 hit.
PF12219. End_tail_spike. 1 hit.
PF03906. Phage_T7_tail. 1 hit.
[Graphical view]
PRINTSPR00849. GLHYDRLASE58.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ858B1.

Entry information

Entry nameQ858B1_BPK1F
AccessionPrimary (citable) accession number: Q858B1
Secondary accession number(s): Q2WC71
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)