opacity-associated protein OapA; This family consists of full-length homologs to OapA, ...
13-438
0e+00
opacity-associated protein OapA; This family consists of full-length homologs to OapA, opacity-associated protein A as described in Haemophilus influenzae. OapA shares a C-terminal homology domain, called the OapA domain, with the Escherichia coli protein YtfB, which is now known to bind peptidoglycan through its OapA domain and to act as a cell division protein.
The actual alignment was detected with superfamily member NF033909:
Pssm-ID: 468239 [Multi-domain] Cd Length: 421 Bit Score: 545.61 E-value: 0e+00
opacity-associated protein OapA; This family consists of full-length homologs to OapA, ...
13-438
0e+00
opacity-associated protein OapA; This family consists of full-length homologs to OapA, opacity-associated protein A as described in Haemophilus influenzae. OapA shares a C-terminal homology domain, called the OapA domain, with the Escherichia coli protein YtfB, which is now known to bind peptidoglycan through its OapA domain and to act as a cell division protein.
Pssm-ID: 468239 [Multi-domain] Cd Length: 421 Bit Score: 545.61 E-value: 0e+00
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the ...
358-438
4.30e-34
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the Haemophilus influenzae protein OapA, which is required for the expression of colony opacity, thus opacity- associated protein A. The OapA protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation. The OapA domain has been shown to bind to peptidoglycan in the E. coli protein YtfB. A screen to identify factors that affect cell division in E. coli discovered that overproducing a fragment of YtfB, including its OapA domain, caused cells to grow as long filaments. OapA domains are commonly associated with other domains that are involved in breaking peptidoglycan cross-links. The OapA domain is distantly related to pfam01476.
Pssm-ID: 427799 [Multi-domain] Cd Length: 85 Bit Score: 122.46 E-value: 4.30e-34
opacity-associated protein OapA; This family consists of full-length homologs to OapA, ...
13-438
0e+00
opacity-associated protein OapA; This family consists of full-length homologs to OapA, opacity-associated protein A as described in Haemophilus influenzae. OapA shares a C-terminal homology domain, called the OapA domain, with the Escherichia coli protein YtfB, which is now known to bind peptidoglycan through its OapA domain and to act as a cell division protein.
Pssm-ID: 468239 [Multi-domain] Cd Length: 421 Bit Score: 545.61 E-value: 0e+00
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the ...
358-438
4.30e-34
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the Haemophilus influenzae protein OapA, which is required for the expression of colony opacity, thus opacity- associated protein A. The OapA protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation. The OapA domain has been shown to bind to peptidoglycan in the E. coli protein YtfB. A screen to identify factors that affect cell division in E. coli discovered that overproducing a fragment of YtfB, including its OapA domain, caused cells to grow as long filaments. OapA domains are commonly associated with other domains that are involved in breaking peptidoglycan cross-links. The OapA domain is distantly related to pfam01476.
Pssm-ID: 427799 [Multi-domain] Cd Length: 85 Bit Score: 122.46 E-value: 4.30e-34
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.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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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)
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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.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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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
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