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UniProt functional annotation for Q04830 | ||
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| UniProt code: Q04830. |
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| Organism: | |
Escherichia phage K1F (Bacteriophage K1F). |
| Taxonomy: | |
Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Autographiviridae; Studiervirinae; Kayfunavirus; Escherichia virus K1F. |
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| Function: | |
[Tail spike protein]: Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid. {ECO:0000269|PubMed:20096705, ECO:0000269|PubMed:3546309}. |
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| Function: | |
[C-terminal chaperone protein]: The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer. {ECO:0000269|PubMed:12556457}. |
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| Catalytic activity: | |
Reaction=Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.; EC=3.2.1.129; Evidence={ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967, ECO:0000269|PubMed:3546309}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=71 uM for poly-alpha-2,8-sialosyl carbohydrates {ECO:0000269|PubMed:3546309}; KM=1.2 mM for oligo-alpha-2,8-sialosyl carbohydrates {ECO:0000269|PubMed:3546309}; KM=7.1 uM for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates {ECO:0000269|PubMed:3546309}; Vmax=19 umol/min/mg enzyme for poly-alpha-2,8-sialosyl carbohydrates cleavage {ECO:0000269|PubMed:3546309}; Vmax=18 umol/min/mg enzyme for oligo-alpha-2,8-sialosyl carbohydrates cleavage {ECO:0000269|PubMed:3546309}; Vmax=13 umol/min/mg enzyme for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates {ECO:0000269|PubMed:3546309}; |
| Subunit: | |
[Tail spike protein]: Homotrimer (PubMed:3546309, PubMed:20124697). Interacts with sialic acid (PubMed:15608653, PubMed:20096705). {ECO:0000269|PubMed:15608653, ECO:0000269|PubMed:20096705, ECO:0000269|PubMed:20124697, ECO:0000269|PubMed:3546309}. |
| Subcellular location: | |
[Tail spike protein]: Virion. Note=Tail spike. {ECO:0000269|PubMed:8331067}. |
| Ptm: | |
Proteolytic cleavage and release of the chaperone stabilizes the folded protein. {ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967}. |
| Similarity: | |
Belongs to the glycosyl hydrolase 58 family. {ECO:0000305}. |
| Sequence caution: | |
Sequence=AAC37340.1; Type=Frameshift; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.