Protein

UniProt accession
Q04830 [UniProt]
Protein name
Tail spike protein
RBP type
TSP
Evidence DepoScope
Probability 1,00
TSP
Evidence RBPdetect
Probability 0,90
TSP
Evidence RBPdetect2
Probability 0,94
TSP
Evidence GenBank
Probability 1,00
TSP
Evidence Phold
Probability 1,00
Protein sequence
MSTITQFPSGNTQYRIEFDYLARTFVVVTLVNSSNPTLNRVLEVGRDYRFLNPTMIEMLVDQSGFDIVRIHRQTGTDLVVDFRNGSVLTASDLTTAELQAIHIAEEGRDQTVDLAKEYADAAGSSAGNAKDSEDEARRIAESIRAAGLIGYMTRRSFEKGYNVTTWSEVLLWEEDGDYYRWDGTLPKNVPAGSTPETSGGIGLGAWVSVGDAALRSQISNPEGAILYPELHRARWLDEKDARGWGAKGDGVTDDTAALTSALNDTPVGQKINGNGKTYKVTSLPDISRFINTRFVYERIPGQPLYYASEEFVQGELFKITDTPYYNAWPQDKAFVYENVIYAPYMGSDRHGVSRLHVSWVKSGDDGQTWSTPEWLTDLHPDYPTVNYHCMSMGVCRNRLFAMIETRTLAKNALTNCALWDRPMSRSLHLTGGITKAANQRYATIHVPDHGLFVGDFVNFSNSAVTGVSGDMTVATVIDKDNFTVLTPNQQTSDLNNAGKNWHMGTSFHKSPWRKTDLGLIPSVTEVHSFATIDNNGFAMGYHQGDVAPREVGLFYFPDAFNSPSNYVRRQIPSEYEPDASEPCIKYYDGVLYLITRGTRGDRLGSSLHRSRDIGQTWESLRFPHNVHHTTLPFAKVGDDLIMFGSERAENEWEAGAPDDRYKASYPRTFYARLNVNNWNADDIEWVNITDQIYQGGIVNSGVGVGSVVVKDNYIYYMFGGEDHFNPWTYGDNSAKDPFKSDGHPSDLYCYKMKIGPDNRVSRDFRYGAVPNRAVPVFFDTNGVRTVPAPMEFTGDLGLGHVTIRASTSSNIRSEVLMEGEYGFIGKSIPTDNPAGQRIIFCGGEGTSSTTGAQITLYGANNTDSRRIVYNGDEHLFQSADVKPYNDNVTALGGPSNRFTTAYLGSNPIVTSNGERKTEPVVFDDAFLDAWGDVHYIMYQWLDAVQLKGNDARIHFGVIAQQIRDVFIAHGLMDENSTNCRYAVLCYDKYPRMTDTVFSHNEIVEHTDEEGNVTTTEEPVYTEVVIHEEGEEWGVRPDGIFFAEAAYQRRKLERIEARLSALEQK
Physico‐chemical
properties
protein length:1064 AA
molecular weight: 118903,57500 Da
isoelectric point:5,10911
aromaticity:0,10996
hydropathy:-0,46241

Domains

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage K1F
[NCBI] 		344021 Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes
Host Escherichia coli
[NCBI] 		562 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Gene Ontology

Description Category Evidence (source)
GO:0098024 virus tail, fiber Cellular Component IDA:UniProtKB (UniProt)
GO:0016996 endo-alpha-(2,8)-sialidase activity Molecular Function IDA:UniProtKB (UniProt)
GO:0042802 identical protein binding Molecular Function IPI:IntAct (UniProt)
GO:0098671 adhesion receptor-mediated virion attachment to host cell Biological Process IEA:UniProtKB-KW (UniProt)
GO:0044409 symbiont entry into host Biological Process IDA:UniProtKB (UniProt)
GO:0098994 symbiont entry into host cell via disruption of host cell envelope Biological Process IEA:UniProtKB-KW (UniProt)
GO:0098996 symbiont entry into host cell via disruption of host cell glycocalyx Biological Process IEA:UniProtKB-KW (UniProt)
GO:0019062 virion attachment to host cell Biological Process IDA:UniProtKB (UniProt)

Enzymatic activity

No enzymatic activity data available.

Tertiary structure

PDB ID
1V0E
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
1V0F
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
3GVJ
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
3GVK
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
3GVL
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
3GW6
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
3JU4
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
View on RCSB Download PDB
PDB ID
8390e9afd841196d5d9924584865e9b67070d6caaffa5682dc814f101130dea4
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,6699
Evidence 0,6699
Download PDB

Literature

Title Authors Date PMID Source
Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. Stummeyer K, Dickmanns A, Mühlenhoff M, Gerardy-Schahn R, Ficner R 2005-01 15608653 PubMed
Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA 1987-03-15 3546309 PubMed
Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. Schulz EC, Schwarzer D, Frank M, Stummeyer K, Mühlenhoff M, Dickmanns A, Gerardy-Schahn R, Ficner R 2010-03-19 20096705 PubMed
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, Mühlenhoff M, Gerardy-Schahn R 2009-04-03 19189967 PubMed
Complete nucleotide sequence of the bacteriophage K1F tail gene encoding endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in bacteriophage PK1E. Petter JG, Vimr ER 1993-07 8331067 PubMed
Structure analysis of endosialidase NF at 0.98 A resolution. Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R 2010-02 20124697 PubMed
Proteolytic processing and oligomerization of bacteriophage-derived endosialidases. Mühlenhoff M, Stummeyer K, Grove M, Sauerborn M, Gerardy-Schahn R 2003-04-11 12556457 PubMed
Complete nucleotide sequence of the bacteriophage K1F tail gene encoding endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in bacteriophage PK1E J G Petter, E R Vimr 1993-07 10.1128/jb.175.14.4354-4363.1993 DOI
Structure analysis of endosialidase NF at 0.98 Å resolution Eike C. Schulz, Piotr Neumann, Rita Gerardy-Schahn, George M. Sheldrick, Ralf Ficner 2010-01-22 10.1107/s0907444909048720 DOI
Structural Basis for the Recognition and Cleavage of Polysialic Acid by the Bacteriophage K1F Tailspike Protein EndoNF Eike Christian Schulz, David Schwarzer, Martin Frank, Katharina Stummeyer, Martina Mühlenhoff, Achim Dickmanns, Rita Gerardy-Schahn, Ralf Ficner 2010-03 10.1016/j.jmb.2010.01.028 DOI
Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. P.C. Hallenbeck, E.R. Vimr, F. Yu, B. Bassler, F.A. Troy 1987-03 10.1016/s0021-9258(18)61387-0 DOI
Proteolytic Release of the Intramolecular Chaperone Domain Confers Processivity to Endosialidase F David Schwarzer, Katharina Stummeyer, Thomas Haselhorst, Friedrich Freiberger, Bastian Rode, Melanie Grove, Thomas Scheper, Mark von Itzstein, Martina Mühlenhoff, Rita Gerardy-Schahn 2009-04 10.1074/jbc.m808475200 DOI
Crystal structure of the polysialic acid–degrading endosialidase of bacteriophage K1F Katharina Stummeyer, Achim Dickmanns, Martina Mühlenhoff, Rita Gerardy-Schahn, Ralf Ficner 2004-12-19 10.1038/nsmb874 DOI
Proteolytic Processing and Oligomerization of Bacteriophage-derived Endosialidases Martina Mühlenhoff, Katharina Stummeyer, Melanie Grove, Markus Sauerborn, Rita Gerardy-Schahn 2003-04 10.1074/jbc.m212048200 DOI