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Q858B1

- Q858B1_BPK1F

UniProt

Q858B1 - Q858B1_BPK1F

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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

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:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF
60 70 80 90 100
LNPTMIEMLV DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA
110 120 130 140 150
IHIAEEGRDQ TVDLAKEYAD AAGSSAGNAK DSEDEARRIA ESIRAAGLIG
160 170 180 190 200
YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR WDGTLPKNVP AGSTPETSGG
210 220 230 240 250
IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD ARGWGAKGDG
260 270 280 290 300
VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP
310 320 330 340 350
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH
360 370 380 390 400
GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF
410 420 430 440 450
AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG
460 470 480 490 500
LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN
510 520 530 540 550
WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG YHQGDVAPRE
560 570 580 590 600
VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG
610 620 630 640 650
DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN
660 670 680 690 700
EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS
710 720 730 740 750
GVGVGSVVVK DNYIYYMFGG EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY
760 770 780 790 800
KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT NGVRTVPAPM EFTGDLGLGH
810 820 830 840 850
VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF CGGEGTSSTT
860 870 880 890 900
GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT
910 920 930 940 950
AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND
960 970 980 990 1000
ARIHFGVIAQ QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN
1010 1020 1030 1040 1050
EIVEHTDEEG NVTTTEEPVY TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK
1060
LERIEARLSA LEQK
Length:1,064
Mass (Da):118,905
Last modified:June 1, 2003 - v1
Checksum:i82FAB75EDC68DAB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
  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 29, 2014
This is version 83 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