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 associating with outer membrane; SusD is a secreted starch-binding protein with ...
31-525
2.59e-31
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.
The actual alignment was detected with superfamily member pfam12771:
Pssm-ID: 463695 Cd Length: 415 Bit Score: 125.97 E-value: 2.59e-31
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with ...
31-525
2.59e-31
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: 125.97 E-value: 2.59e-31
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
85-311
2.65e-12
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: 68.21 E-value: 2.65e-12
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with ...
31-525
2.59e-31
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: 125.97 E-value: 2.59e-31
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member ...
91-544
2.24e-18
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: 88.10 E-value: 2.24e-18
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
85-311
2.65e-12
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: 68.21 E-value: 2.65e-12
Starch-binding associating with outer membrane; SusD is a secreted polysaccharide-binding ...
27-192
4.25e-03
Starch-binding associating with outer membrane; SusD is a secreted polysaccharide-binding protein with an N-terminal lipid moiety that allows it to associate with the outer membrane. SusD probably mediates xyloglucan-binding prior to xyloglucan transport in the periplasm for degradation. This domain is found N-terminal to pfam07980.
Pssm-ID: 405073 Cd Length: 185 Bit Score: 38.55 E-value: 4.25e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
(CDART).
Modify your query to search against a different database and/or use advanced search options
