RagB/SusD family nutrient uptake outer membrane protein similar to Bacteroides thetaiotaomicron starch-binding protein SusD, which is a major starch-binding protein present at the surface of the cell and mediates starch-binding before starch transport in the periplasm for degradation
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
27-510
0e+00
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.
The actual alignment was detected with superfamily member pfam12741:
Pssm-ID: 451378 Cd Length: 495 Bit Score: 603.50 E-value: 0e+00
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member ...
27-510
0e+00
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member of which, BT1043, is an outer membrane lipoprotein involved in host glycan metabolism. The structures of this and SusD-homologs in the family are dominated by tetratrico peptide repeats that may facilitate association with outer membrane beta-barrel transporters required for glycan uptake. The structure of BT1043 complexed with N-acetyllactosamine reveals that recognition is mediated via hydrogen bonding interactions with the reducing end of beta-N-acetylglucosamine, suggesting a role in binding glycans liberated from the mucin polypeptide. Mammalian distal gut bacteria have an expanded capacity to utilize glycans. In the absence of dietary sources, some species rely on host-derived mucosal glycans. The ability of Bacteroides thetaiotaomicron, a prominent human gut symbiont, to forage host glycans contributes to both its ability to persist within an individual host and its ability to be transmitted naturally to new hosts at birth.
Pssm-ID: 432756 Cd Length: 495 Bit Score: 603.50 E-value: 0e+00
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
123-452
1.67e-26
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.
Pssm-ID: 185760 [Multi-domain] Cd Length: 359 Bit Score: 110.59 E-value: 1.67e-26
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member ...
27-510
0e+00
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member of which, BT1043, is an outer membrane lipoprotein involved in host glycan metabolism. The structures of this and SusD-homologs in the family are dominated by tetratrico peptide repeats that may facilitate association with outer membrane beta-barrel transporters required for glycan uptake. The structure of BT1043 complexed with N-acetyllactosamine reveals that recognition is mediated via hydrogen bonding interactions with the reducing end of beta-N-acetylglucosamine, suggesting a role in binding glycans liberated from the mucin polypeptide. Mammalian distal gut bacteria have an expanded capacity to utilize glycans. In the absence of dietary sources, some species rely on host-derived mucosal glycans. The ability of Bacteroides thetaiotaomicron, a prominent human gut symbiont, to forage host glycans contributes to both its ability to persist within an individual host and its ability to be transmitted naturally to new hosts at birth.
Pssm-ID: 432756 Cd Length: 495 Bit Score: 603.50 E-value: 0e+00
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with ...
35-480
1.61e-76
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.
Pssm-ID: 463695 Cd Length: 415 Bit Score: 246.54 E-value: 1.61e-76
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
123-452
1.67e-26
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.
Pssm-ID: 185760 [Multi-domain] Cd Length: 359 Bit Score: 110.59 E-value: 1.67e-26
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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