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    Biotechnology Information genbank accession numbers
    Genbank Accession Numbers, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 1 article reviews
    genbank accession numbers - by Bioz Stars, 2026-02
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    ncbi/genbank accession # ear30327  (Biotechnology Information)
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    Biotechnology Information ncbi/genbank accession # ear30327
    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 .
    Ncbi/Genbank Accession # Ear30327, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    genbank accession number: oq938270  (Biotechnology Information)
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    Biotechnology Information genbank accession number: oq938270
    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