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Q858B1

- Q858B1_BPK1F

UniProt

Q858B1 - Q858B1_BPK1F

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Protein
Submitted name: Endo-N-acetylneuraminidase
Gene
sia, 17, 17.0
Organism
Enterobacteria phage K1F (Bacteriophage K1F)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei819 – 8191Phosphate 1; via amide nitrogenImported
Binding sitei819 – 8191Phosphate 2; via amide nitrogenImported
Binding sitei819 – 8191Phosphate 3; via amide nitrogenImported
Binding sitei830 – 8301Phosphate 1Imported
Binding sitei830 – 8301Phosphate 4Imported

GO - Molecular functioni

  1. endo-alpha-(2,8)-sialidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseImported, Hydrolase

Protein family/group databases

CAZyiGH58. Glycoside Hydrolase Family 58.
MEROPSiS74.001.

Names & Taxonomyi

Protein namesi
Submitted name:
Endo-N-acetylneuraminidaseImported
Submitted name:
Endo-alpha-sialidaseImported (EC:3.2.1.129Imported)
Submitted name:
Precursor of gp17Imported (EC:3.2.1.129Imported)
Gene namesi
Name:siaImported
Synonyms:17Imported, 17.0Imported
OrganismiEnterobacteria phage K1F (Bacteriophage K1F)Imported
Taxonomic identifieri344021 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000001530: Genome, UP000001722: Genome

Interactioni

Protein-protein interaction databases

DIPiDIP-48774N.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0EX-ray1.90A/B/C/D/E/F246-910[»]
1V0FX-ray2.55A/B/C/D/E/F246-910[»]

Miscellaneous databases

EvolutionaryTraceiQ858B1.

Family & Domainsi

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProiIPR023366. 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]
PfamiPF12195. 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]
PRINTSiPR00849. GLHYDRLASE58.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q858B1-1 [UniParc]FASTAAdd to Basket

« Hide

MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF     50
LNPTMIEMLV DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA 100
IHIAEEGRDQ TVDLAKEYAD AAGSSAGNAK DSEDEARRIA ESIRAAGLIG 150
YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR WDGTLPKNVP AGSTPETSGG 200
IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD ARGWGAKGDG 250
VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP 300
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH 350
GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF 400
AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG 450
LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN 500
WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG YHQGDVAPRE 550
VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG 600
DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN 650
EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS 700
GVGVGSVVVK DNYIYYMFGG EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY 750
KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT NGVRTVPAPM EFTGDLGLGH 800
VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF CGGEGTSSTT 850
GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT 900
AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND 950
ARIHFGVIAQ QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN 1000
EIVEHTDEEG NVTTTEEPVY TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK 1050
LERIEARLSA LEQK 1064
Length:1,064
Mass (Da):118,905
Last modified:June 1, 2003 - v1
Checksum:i82FAB75EDC68DAB6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ111067 Genomic DNA. Translation: AAZ73001.1.
AJ505988 Genomic DNA. Translation: CAD44528.2.
AM084414 Genomic DNA. Translation: CAJ29390.1.
RefSeqiYP_338127.1. NC_007456.1.

Genome annotation databases

GeneIDi3707741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ111067 Genomic DNA. Translation: AAZ73001.1 .
AJ505988 Genomic DNA. Translation: CAD44528.2 .
AM084414 Genomic DNA. Translation: CAJ29390.1 .
RefSeqi YP_338127.1. NC_007456.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V0E X-ray 1.90 A/B/C/D/E/F 246-910 [» ]
1V0F X-ray 2.55 A/B/C/D/E/F 246-910 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48774N.

Protein family/group databases

CAZyi GH58. Glycoside Hydrolase Family 58.
MEROPSi S74.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3707741.

Miscellaneous databases

EvolutionaryTracei Q858B1.

Family and domain databases

Gene3Di 2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProi IPR023366. 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 ]
Pfami PF12195. 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 ]
PRINTSi PR00849. GLHYDRLASE58.
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "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.
  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. 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. Cited for: NUCLEOTIDE SEQUENCE OF 790-1064.

Entry informationi

Entry nameiQ858B1_BPK1F
AccessioniPrimary (citable) accession number: Q858B1
Secondary accession number(s): Q2WC71
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome

External Data

Dasty 3

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