Difference between revisions of "Part:BBa K5246022"
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<partinfo>BBa_K5246022 short</partinfo> | <partinfo>BBa_K5246022 short</partinfo> | ||
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===Introduction=== | ===Introduction=== | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | Gene HfsJ from Hirschia baltica encodes a protein of 260 amino acids. HfsJ is one of the glycosyltransferases involved in holdfast synthesis pathway and is structurally very similar to glycosyltransferases that transfer UDP-N-acetyl-D-mannosaminuronic acid. Ir belongs to the WecB/TagA/CpsF family of glycosyltransferases that catalyze the formation of glycosidic bonds and may be involved in the biosynthesis of repeating polysaccharide units found in membrane glycolipids. | + | Gene HfsJ from Hirschia baltica encodes a protein of 260 amino acids. HfsJ is one of the glycosyltransferases involved in the holdfast synthesis pathway and is structurally very similar to glycosyltransferases that transfer UDP-N-acetyl-D-mannosaminuronic acid. Ir belongs to the WecB/TagA/CpsF family of glycosyltransferases that catalyze the formation of glycosidic bonds and may be involved in the biosynthesis of repeating polysaccharide units found in membrane glycolipids. |
It is predicted that this is an intracellular protein. | It is predicted that this is an intracellular protein. | ||
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<partinfo>BBa_K5246022 SequenceAndFeatures</partinfo> | <partinfo>BBa_K5246022 SequenceAndFeatures</partinfo> | ||
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===Experimental characterization=== | ===Experimental characterization=== | ||
| + | ====Bioinformatic analysis==== | ||
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| + | CDD analysis revealed that HfsJ is part of the WecB/TgA/CpsF glycosyltransferase family. This family catalyzes the formation of glycosidic bonds and may be involved in the biosynthesis of repeating polysaccharide units found in membrane glycolipids. It has domains very similar to E.Coli WecG glycosyltransferase, which is responsible for UDP-N-acetyl-D-mannosaminuronic acid transfer. Results are supported by the protein BLAST, which showed significant similarities with the same WecG glycosyltransferase from E.Coli. | ||
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| + | DeepTMHMM analysis predicted that HfsJ is a globular protein located on the cytoplasmic side of the membrane. | ||
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| + | AlphaFold 3 structure, with a high confidence score, shows that HfsJ is most likely a globular protein mostly made of alpha helices. A pTM score above 0.5 suggests that the predicted overall structure may closely resemble the true protein fold, while ipTM indicates the accuracy of the subunit positioning within the complex. Values higher than 0.8 represent confident, high-quality predictions. | ||
| + | |||
| + | Based on our findings and prior research, we propose that HfsJ is likely a globular protein responsible for transferring UDP-N-acetyl-D-mannosaminuronic acid and catalyzing the formation of a glycosidic bond. [1][2] | ||
===References=== | ===References=== | ||
| + | 1. Toh, E., Kurtz, Harry D. and Brun, Y.V. (2008) ‘Characterization of the Caulobacter crescentus holdfast polysaccharide biosynthesis pathway reveals significant redundancy in the initiating glycosyltransferase and polymerase steps’, Journal of Bacteriology, 190(21), pp. 7219–7231. doi:10.1128/jb.01003-08. | ||
| + | <br> | ||
| + | 2. Chepkwony, N.K., Berne, C. and Brun, Y.V. (2019b) ‘Comparative analysis of ionic strength tolerance between freshwater and marine Caulobacterales adhesins’, Journal of Bacteriology, 201(18). doi:10.1128/jb.00061-19. | ||
Revision as of 11:36, 28 September 2024
HB HfsJ Glycosyltransferase
Introduction
Usage and Biology
Gene HfsJ from Hirschia baltica encodes a protein of 260 amino acids. HfsJ is one of the glycosyltransferases involved in the holdfast synthesis pathway and is structurally very similar to glycosyltransferases that transfer UDP-N-acetyl-D-mannosaminuronic acid. Ir belongs to the WecB/TagA/CpsF family of glycosyltransferases that catalyze the formation of glycosidic bonds and may be involved in the biosynthesis of repeating polysaccharide units found in membrane glycolipids. It is predicted that this is an intracellular protein.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 188
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 188
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 622
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 188
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 188
- 1000COMPATIBLE WITH RFC[1000]
Experimental characterization
Bioinformatic analysis
CDD analysis revealed that HfsJ is part of the WecB/TgA/CpsF glycosyltransferase family. This family catalyzes the formation of glycosidic bonds and may be involved in the biosynthesis of repeating polysaccharide units found in membrane glycolipids. It has domains very similar to E.Coli WecG glycosyltransferase, which is responsible for UDP-N-acetyl-D-mannosaminuronic acid transfer. Results are supported by the protein BLAST, which showed significant similarities with the same WecG glycosyltransferase from E.Coli.
DeepTMHMM analysis predicted that HfsJ is a globular protein located on the cytoplasmic side of the membrane.
AlphaFold 3 structure, with a high confidence score, shows that HfsJ is most likely a globular protein mostly made of alpha helices. A pTM score above 0.5 suggests that the predicted overall structure may closely resemble the true protein fold, while ipTM indicates the accuracy of the subunit positioning within the complex. Values higher than 0.8 represent confident, high-quality predictions.
Based on our findings and prior research, we propose that HfsJ is likely a globular protein responsible for transferring UDP-N-acetyl-D-mannosaminuronic acid and catalyzing the formation of a glycosidic bond. [1][2]
References
1. Toh, E., Kurtz, Harry D. and Brun, Y.V. (2008) ‘Characterization of the Caulobacter crescentus holdfast polysaccharide biosynthesis pathway reveals significant redundancy in the initiating glycosyltransferase and polymerase steps’, Journal of Bacteriology, 190(21), pp. 7219–7231. doi:10.1128/jb.01003-08.
2. Chepkwony, N.K., Berne, C. and Brun, Y.V. (2019b) ‘Comparative analysis of ionic strength tolerance between freshwater and marine Caulobacterales adhesins’, Journal of Bacteriology, 201(18). doi:10.1128/jb.00061-19.