Q858B1 (Q858B1_BPK1F) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Endo-N-acetylneuraminidase EMBL AAZ73001.1

Submitted name:
Endo-alpha-sialidase EMBL CAD44528.2
EC=3.2.1.129 EMBL CAD44528.2
Submitted name:
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

Organism

Enterobacteria phage K1F (Bacteriophage K1F) EMBL CAD44528.2

Taxonomic identifier

344021 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › Autographivirinae › T7-like viruses

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	1064 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Glycosidase EMBL CAD44528.2 Hydrolase
Technical term	3D-structure PDB 1V0E PDB 1V0F
Gene Ontology (GO)
Molecular function	endo-alpha-(2,8)-sialidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q858B1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 82FAB75EDC68DAB6	FASTA	1,064	118,905
	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

References

[1]	"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: 16689790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"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: 20096705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 2-910.
[3]	"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 Biol. Crystallogr. 66:176-180(2010) [PubMed: 20124697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 2-910.
[4]	"Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding." Schulz E.C., Dickmanns A., Urlaub H., Schmitt A., Muehlenhoff M., Stummeyer K., Schwarzer D., Gerardy-Schahn R., Ficner R. Nat. Struct. Mol. Biol. 17:210-215(2010) [PubMed: 20118935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 790-1064.
[5]	"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: 19189967] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 2-1064.
[6]	"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: 17158460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 2-1064.
[7]	"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: 16991177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 2-910.
[8]	"Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F." Stummeyer K., Dickmanns A., M hlenhoff.M., Gerardy-Schahn R., Ficner R. Nat. Struct. Mol. Biol. 12:90-96(2005) [PubMed: 15608653] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 246-910.
[9]	"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.
[10]	"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: 16321955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[11]	"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: 12556457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.

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.

RefSeq

YP_338127.1. NC_007456.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q858B1.

SMR

Q858B1. Positions 246-910.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48774N.

Protein family/group databases

CAZy

GH58. Glycoside Hydrolase Family 58.

MEROPS

S74.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3707741.

GenomeReviews

Gene locus sia in contig AM084414_GR.
Gene locus sia in contig DQ111067_GR.

Phylogenomic databases

ProtClustDB

CLSP988200.

Family and domain databases

InterPro

IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR024427. Endosialidase_beta_barrel.
IPR024428. Endosialidase_beta_prop.
IPR024430. Endosialidase_C.
IPR024429. Endosialidase_N-extension.
IPR001724. Glyco_hydro_58.
IPR011040. Neuraminidase.
IPR005604. Phage_T7_tail_fibre.
[Graphical view]

Gene3D

G3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
G3DSA:3.30.750.60. G3DSA:3.30.750.60. 1 hit.
G3DSA:4.10.1090.10. G3DSA:4.10.1090.10. 1 hit.
G3DSA:2.120.10.10. Neuraminidase. 2 hits.

Pfam

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]

PRINTS

PR00849. GLHYDRLASE58.

SUPFAM

SSF50939. Sialidase. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q858B1_BPK1F

Accession

Primary (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:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)