Protein

UniProt accession
Q9AYY6 [UniProt]
Protein name
Tail spike protein
RBP type
TSP

evidence: UniProt/TrEMBL

probability: 1,0000

TSP

evidence: DepoScope

probability: 1,0000

TSP

evidence: RBPdetect

probability: 0,9463

TSP

evidence: RBPdetect2

probability: 0,9481

Protein sequence
MTDSINANVVVSMPSQLFTMARSFKAVANGKIYIGKIDTDPVNPENRIQVYVENEDGSHVPVSQPIIINAAGYPVYNGQIAKFVTVQGHSMAVYDAYGAQQFYFPNVLKYDPDQFRAIIESPEGAGHVGYQYRRNTGSTMRMVSDVLDERVSLWDFHCDPSGNVIQPGPNVDSRQYLQAAIDYVSSNGGGTITIPAGYTWYLGSYGVGGIAGHSGIIQLRSNVNLNIEGRIHLSPFFDLKPFQVFVGFDNGDPASSGNLENCHIYGHGVVDFGGYEFGASSQLRNGVAFGRSYNCSVTGITFQNGDVTWAITLGWNGYGSNCYVRKCRFINLVNSSVNADHSTVYVNCPYSGVESCYFSMSSSFARNIACSVELHQHDTFYRGSTVNGYCRGAYVVMHAAEAAGAGSYAYNMQVENNIAVIYGQFVILGSDVTATVSGHLNDVIVSGNIVSIGERAAFSAPFGAFIDIGPDNSGASNVQDIQRVLVTGNSFYAPANITDSAAITLRANLNGCTFIANNFDCRYMVYNAPGTTSPVVQNLVWDKSNVIGGTHANQRAGQNLFDMQFASVVNSTIEVQLSCEDLSMFSCILFPASCQLSYSKITVDSAWTKSMSNTAVFEGNQQAGANVYVSYPATVNLTSYNTQGAVPFFSTDTNYAWVTSAYSLSINENLDFSPPATYTNKANGQLVGVGYNEIGGVRSVSVRLMLQRQV
Physico‐chemical
properties
protein length:710 AA
molecular weight: 76780,69370 Da
isoelectric point:5,27633
aromaticity:0,11549
hydropathy:-0,05014

Domains

Domains [InterPro]
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterobacteria phage HK620
[NCBI]
155148 Uroviricota > Caudoviricetes > Lederbergvirus >
Host Escherichia coli
[NCBI]
562 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AAK28905.1 [NCBI]
Genbank nucleotide accession
AF335538 [NCBI]
CDS location
range 34478 -> 36610
strand +
CDS
ATGACAGATTCAATAAATGCCAATGTTGTAGTGAGCATGCCTTCGCAACTCTTCACTATGGCGCGTTCTTTTAAAGCCGTAGCCAATGGCAAAATTTATATCGGGAAAATTGACACTGATCCGGTAAATCCTGAAAACCGGATTCAGGTTTATGTAGAGAACGAAGACGGCTCTCACGTTCCTGTTTCTCAACCAATCATCATTAACGCTGCTGGTTATCCGGTATATAACGGACAGATTGCCAAATTCGTTACCGTGCAAGGCCATTCTATGGCTGTTTATGATGCATATGGTGCTCAGCAGTTCTATTTTCCTAATGTGCTTAAGTATGACCCTGACCAGTTCAGGGCAATTATAGAGTCACCAGAAGGTGCTGGACACGTAGGATATCAGTATCGCAGGAATACAGGGTCGACCATGAGAATGGTAAGCGATGTGCTGGATGAGCGTGTGAGCCTGTGGGATTTTCATTGTGACCCATCCGGCAATGTAATTCAGCCAGGACCAAACGTTGACAGTCGCCAATATCTACAAGCAGCAATTGATTATGTATCGTCTAATGGAGGTGGAACAATCACCATTCCAGCAGGCTATACGTGGTATCTTGGATCTTATGGTGTTGGAGGAATTGCAGGGCATAGTGGAATTATTCAGTTGCGCAGCAATGTTAATCTAAATATTGAAGGTAGAATTCATCTTTCTCCATTCTTTGACCTTAAGCCATTTCAGGTGTTTGTAGGCTTTGATAATGGCGATCCCGCAAGCTCTGGTAATCTGGAGAACTGCCATATTTATGGGCATGGTGTAGTGGACTTTGGTGGTTATGAGTTTGGAGCATCCAGTCAACTACGTAATGGTGTTGCTTTTGGGCGTAGTTACAATTGTTCTGTAACAGGTATTACTTTCCAGAATGGTGACGTTACTTGGGCTATTACCTTAGGCTGGAATGGGTACGGGTCTAACTGCTACGTGCGCAAGTGCCGCTTTATCAACTTAGTGAACAGCAGTGTCAATGCAGACCACAGTACAGTGTACGTCAACTGCCCCTACAGCGGAGTTGAGTCCTGCTACTTCAGTATGTCTAGTTCATTCGCGCGTAACATCGCGTGCTCTGTAGAGTTGCACCAACATGATACCTTCTACCGCGGAAGTACTGTAAACGGATACTGCCGTGGCGCATATGTAGTTATGCACGCAGCAGAGGCTGCTGGTGCAGGTTCTTATGCTTACAACATGCAGGTTGAAAACAACATCGCGGTCATTTACGGCCAGTTCGTTATATTAGGCTCTGACGTAACTGCTACAGTCTCTGGACATCTTAATGACGTCATCGTATCTGGTAACATCGTAAGTATTGGTGAGCGGGCTGCGTTCTCAGCTCCGTTTGGGGCATTTATTGATATTGGCCCGGACAATAGCGGGGCTAGTAATGTACAAGATATCCAGCGAGTGCTTGTAACAGGCAACAGTTTCTATGCTCCTGCTAACATCACTGATAGTGCTGCAATTACCCTGCGAGCTAATCTTAATGGTTGCACCTTTATCGCTAACAATTTTGATTGCCGTTACATGGTCTACAACGCTCCCGGTACTACAAGCCCTGTAGTTCAGAATCTGGTATGGGATAAGTCCAATGTTATCGGCGGGACTCACGCGAATCAACGTGCAGGACAGAATCTATTTGATATGCAGTTTGCATCTGTAGTAAACAGCACTATAGAAGTACAGCTTAGCTGTGAAGATCTGAGCATGTTTAGCTGCATACTCTTCCCTGCATCATGTCAGTTGTCGTACTCGAAGATAACGGTAGATTCTGCATGGACAAAAAGCATGTCAAATACCGCGGTATTTGAAGGTAATCAACAGGCAGGTGCTAATGTATATGTGTCGTATCCAGCTACCGTTAACCTTACAAGTTACAACACCCAAGGAGCGGTTCCTTTCTTTAGTACAGACACCAACTACGCATGGGTTACCAGCGCCTACTCTTTAAGTATTAACGAAAATTTAGATTTCTCGCCACCAGCTACTTATACCAATAAAGCCAACGGACAGTTGGTTGGGGTTGGGTATAACGAGATAGGTGGGGTGCGTTCAGTTAGTGTGAGGTTGATGCTGCAGCGTCAGGTGTGA

Gene Ontology

Description Category Evidence (source)
GO:0044423 virion component Cellular Component IEA:UniProtKB-KW (UniProt)
GO:0046872 metal ion binding Molecular Function IEA:UniProtKB-KW (UniProt)
GO:0051701 biological process involved in interaction with host Biological Process IEA:UniProtKB-ARBA (UniProt)
GO:0019058 viral life cycle Biological Process IEA:UniProtKB-ARBA (UniProt)

Enzymatic activity

No enzymatic activity data available.

Tertiary structure

PDB ID: 2VJI

Method: PDB

Resolution: 1,0000

Evidence: 1,0000

View on RCSB

Literature

Title Authors Date PMID Source
Solvent Networks Tune Thermodynamics of Oligosaccharide Complex Formation in an Extended Protein Binding Site. Kunstmann S, Gohlke U, Broeker NK, Roske Y, Heinemann U, Santer M, Barbirz S 2018-08-22 30044908 PubMed
Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity. Broeker NK, Gohlke U, Müller JJ, Uetrecht C, Heinemann U, Seckler R, Barbirz S 2013-01 22923442 PubMed
Nucleotide sequence of coliphage HK620 and the evolution of lambdoid phages. Clark AJ, Inwood W, Cloutier T, Dhillon TS 2001-08-24 11518522 PubMed
Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related. Barbirz S, Müller JJ, Uetrecht C, Clark AJ, Heinemann U, Seckler R 2008-07 18547389 PubMed
Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity N. K. Broeker, U. Gohlke, J. J. Muller, C. Uetrecht, U. Heinemann, R. Seckler, S. Barbirz 2012-08-24 10.1093/glycob/cws126 DOI
Nucleotide sequence of coliphage HK620 and the evolution of lambdoid phages Alvin J Clark, W Inwood, T Cloutier, T.S Dhillon 2001-08 10.1006/jmbi.2001.4868 DOI
Crystal structure of <i>Escherichia coli</i> phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related Stefanie Barbirz, Jürgen J. Müller, Charlotte Uetrecht, Alvin J. Clark, Udo Heinemann, Robert Seckler 2008-06-28 10.1111/j.1365-2958.2008.06311.x DOI
Solvent Networks Tune Thermodynamics of Oligosaccharide Complex Formation in an Extended Protein Binding Site Sonja Kunstmann, Ulrich Gohlke, Nina K. Broeker, Yvette Roske, Udo Heinemann, Mark Santer, Stefanie Barbirz 2018-07-25 10.1021/jacs.8b03719 DOI