Gene Ontology annotation through association of InterPro records with GO terms
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The InterPro2GO mappings for cohesin domains (IPR002102) and CBM superfamily (IPR008965) incorrectly assign carbohydrate-related functions to all proteins containing these domains. For SdbA, which contains a type II cohesin that binds dockerin (not carbohydrates), these mappings produce erroneous annotations.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
A new type of cohesin domain that specifically binds the dockerin domain of the Clostridium thermocellum cellulosome-integrating protein CipA
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Original characterization of SdbA identifying the type II cohesin domain and its specific binding to CipA dockerin domain.
"The NH2-terminal region of SdbA and a fusion protein carrying the first NH2-terminal repeat of OlpB were shown to bind the dockerin domain of CipA. Thus, a new type of cohesin domain, which is present in one, two, and four copies in SdbA, ORF2p, and OlpB, respectively, can be defined"
Insights into the structural determinants of cohesin-dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA
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High-resolution (1.8 A) X-ray structure of SdbA cohesin domain (residues 29-191).
"Here we report the crystal structure of the Type II cohesin (CohII) from the Clostridium thermocellum cell surface anchoring protein SdbA. The protein domain contains nine beta-strands and a small alpha-helix"
Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome
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Crystal structure of a ternary complex including SdbA cohesin (residues 27-200).
"Herein, we have used x-ray crystallography and small angle x-ray scattering to structurally characterize a ternary protein complex from the Clostridium thermocellum cellulosome that comprises a C-terminal trimodular fragment of the CipA scaffoldin bound to the SdbA type II cohesin module"
The contribution of cellulosomal scaffoldins to cellulose hydrolysis by Clostridium thermocellum analyzed by using thermotargetrons
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Genetic deletion of sdbA causes 14-25% reduction in cellulose hydrolysis rate.
"Disruptants lacking any of four different secondary scaffoldins (OlpB, 7CohII, Orf2p, or SdbA) showed moderately decreased cellulose hydrolysis rates, suggesting additive contributions"
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Demonstrates functional redundancy among anchoring scaffoldins (SdbA, OlpB, Orf2p).
"Disruptants lacking any of four different secondary scaffoldins (OlpB, 7CohII, Orf2p, or SdbA) showed moderately decreased cellulose hydrolysis rates, suggesting additive contributions"
Deep research review of sdbA (P71143) function
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SdbA is a noncatalytic, cell-surface anchoring scaffoldin with a single type II cohesin and SLH repeats, mediating attachment of CipA-based cellulosomes to the cell envelope.
"SdbA is best annotated as a noncatalytic, cell-surface anchoring scaffoldin with a single type II cohesin and SLH repeats, mediating attachment of CipA-based cellulosomes to the cell envelope
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SdbA type II cohesin binds CipA type II dockerin to anchor the cellulosome.
"SdbA is a cell-surface anchoring scaffoldin that tethers CipA-based cellulosomes to the bacterial envelope via high-affinity binding between CipA C-terminal type II dockerin (XDocII) and the SdbA type II cohesin
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SLH domains mediate cell wall attachment.
"SdbA contains SLH repeats that bind cell envelope components, providing noncovalent anchoring to the bacterial surface
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