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ncbi/genbank accession # ear30327  (Biotechnology Information)
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Sequence and structural analysis predicts <t>EAR30327</t> (BapP) as a Ca 2+ -dependent outer membrane adhesin. ( A ) AlphaFold model of BapP colored by its domain architecture shown in panel B . The predicted structure of BapP consists of an N-terminal Sec/SPI signal peptide (amino acids 1–20), an N-terminal five-bladed propeller, and 12 tandem beta-sandwich repeats. The beta-sandwich repeats can be subdivided into three classes based on alignments shown in panel C . ( D and E ) Predicted Ca 2+ -binding sites (Ca 2+ ions in red) in B2, B3, and R7 domains based on AlphaFold and AlphaFill modeling (see Materials and Methods). Key Ca 2+ -binding residues are also depicted in the alignments in panel C .
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Sequence and structural analysis predicts <t>EAR30327</t> (BapP) as a Ca 2+ -dependent outer membrane adhesin. ( A ) AlphaFold model of BapP colored by its domain architecture shown in panel B . The predicted structure of BapP consists of an N-terminal Sec/SPI signal peptide (amino acids 1–20), an N-terminal five-bladed propeller, and 12 tandem beta-sandwich repeats. The beta-sandwich repeats can be subdivided into three classes based on alignments shown in panel C . ( D and E ) Predicted Ca 2+ -binding sites (Ca 2+ ions in red) in B2, B3, and R7 domains based on AlphaFold and AlphaFill modeling (see Materials and Methods). Key Ca 2+ -binding residues are also depicted in the alignments in panel C .
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Sequence and structural analysis predicts EAR30327 (BapP) as a Ca 2+ -dependent outer membrane adhesin. ( A ) AlphaFold model of BapP colored by its domain architecture shown in panel B . The predicted structure of BapP consists of an N-terminal Sec/SPI signal peptide (amino acids 1–20), an N-terminal five-bladed propeller, and 12 tandem beta-sandwich repeats. The beta-sandwich repeats can be subdivided into three classes based on alignments shown in panel C . ( D and E ) Predicted Ca 2+ -binding sites (Ca 2+ ions in red) in B2, B3, and R7 domains based on AlphaFold and AlphaFill modeling (see Materials and Methods). Key Ca 2+ -binding residues are also depicted in the alignments in panel C .

Journal: mBio

Article Title: Comparative proteomics of biofilm development in Pseudoalteromonas tunicata discovers a distinct family of Ca 2+ -dependent adhesins

doi: 10.1128/mbio.01069-25

Figure Lengend Snippet: Sequence and structural analysis predicts EAR30327 (BapP) as a Ca 2+ -dependent outer membrane adhesin. ( A ) AlphaFold model of BapP colored by its domain architecture shown in panel B . The predicted structure of BapP consists of an N-terminal Sec/SPI signal peptide (amino acids 1–20), an N-terminal five-bladed propeller, and 12 tandem beta-sandwich repeats. The beta-sandwich repeats can be subdivided into three classes based on alignments shown in panel C . ( D and E ) Predicted Ca 2+ -binding sites (Ca 2+ ions in red) in B2, B3, and R7 domains based on AlphaFold and AlphaFill modeling (see Materials and Methods). Key Ca 2+ -binding residues are also depicted in the alignments in panel C .

Article Snippet: The top-ranked protein overall in both was National Center for Biotechnology Information (NCBI)/GenBank accession # EAR30327 ( ; ), a hypothetical protein that we targeted for subsequent experimental characterization.

Techniques: Sequencing, Membrane, Binding Assay