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Q858B1

- Q858B1_BPK1F

UniProt

Q858B1 - Q858B1_BPK1F

Protein
Submitted name:

Endo-N-acetylneuraminidase

Gene

sia

Organism
Enterobacteria phage K1F (Bacteriophage K1F)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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

    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[»]
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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.
    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 [LARGE SCALE GENOMIC DNA].
    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: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteomeImported

    External Data

    Dasty 3