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genome sequenced f alocis type strain  (ATCC)


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    Structured Review

    ATCC genome sequenced f alocis type strain
    ( A ) Overlapping conserved domains in the FtxA protein sequence, deduced using InterPro. The C-terminal portion displays homology to the Hemolysin-type calcium binding-related domain (IPR010566), and the serralysin-like metalloprotease superfamily (IPR011049), and contains repeats-in-toxins (RTX) calcium-binding nonapeptide repeats (IPR001343), and Hemolysin-type calcium-binding conserved sites (IPR018511). ( B ) One archetypal RTX gene cluster ( hlyCABD ) encodes the E. coli alpha-hemolysin, HlyA. HlyA is synthesized as an inactive protoxin, ProHlyA, which is post-translationally activated in two steps, first via HlyC-directed acylation in the cytoplasm, and then by binding Ca 2+ in the extracellular medium . The cyaE gene of B. pertussis encodes a homologue to E. coli tolC and plays a critical role in the secretion of CyaA . We identified no equivalent to an HlyC-homologue in the F. <t>alocis</t> genomes. The hypothetical protein encoded upstream of ftxA exhibits no apparent homology to hlyC or to other known proteins.
    Genome Sequenced F Alocis Type Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 96 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/genome+sequenced+f+alocis+type+strain/pmc07692872-10-9-14?v=ATCC
    Average 96 stars, based on 96 article reviews
    genome sequenced f alocis type strain - by Bioz Stars, 2026-08
    96/100 stars

    Images

    1) Product Images from "Phylogenetic Analysis of Filifactor alocis Strains Isolated from Several Oral Infections Identified a Novel RTX Toxin, FtxA"

    Article Title: Phylogenetic Analysis of Filifactor alocis Strains Isolated from Several Oral Infections Identified a Novel RTX Toxin, FtxA

    Journal: Toxins

    doi: 10.3390/toxins12110687

    ( A ) Overlapping conserved domains in the FtxA protein sequence, deduced using InterPro. The C-terminal portion displays homology to the Hemolysin-type calcium binding-related domain (IPR010566), and the serralysin-like metalloprotease superfamily (IPR011049), and contains repeats-in-toxins (RTX) calcium-binding nonapeptide repeats (IPR001343), and Hemolysin-type calcium-binding conserved sites (IPR018511). ( B ) One archetypal RTX gene cluster ( hlyCABD ) encodes the E. coli alpha-hemolysin, HlyA. HlyA is synthesized as an inactive protoxin, ProHlyA, which is post-translationally activated in two steps, first via HlyC-directed acylation in the cytoplasm, and then by binding Ca 2+ in the extracellular medium . The cyaE gene of B. pertussis encodes a homologue to E. coli tolC and plays a critical role in the secretion of CyaA . We identified no equivalent to an HlyC-homologue in the F. alocis genomes. The hypothetical protein encoded upstream of ftxA exhibits no apparent homology to hlyC or to other known proteins.
    Figure Legend Snippet: ( A ) Overlapping conserved domains in the FtxA protein sequence, deduced using InterPro. The C-terminal portion displays homology to the Hemolysin-type calcium binding-related domain (IPR010566), and the serralysin-like metalloprotease superfamily (IPR011049), and contains repeats-in-toxins (RTX) calcium-binding nonapeptide repeats (IPR001343), and Hemolysin-type calcium-binding conserved sites (IPR018511). ( B ) One archetypal RTX gene cluster ( hlyCABD ) encodes the E. coli alpha-hemolysin, HlyA. HlyA is synthesized as an inactive protoxin, ProHlyA, which is post-translationally activated in two steps, first via HlyC-directed acylation in the cytoplasm, and then by binding Ca 2+ in the extracellular medium . The cyaE gene of B. pertussis encodes a homologue to E. coli tolC and plays a critical role in the secretion of CyaA . We identified no equivalent to an HlyC-homologue in the F. alocis genomes. The hypothetical protein encoded upstream of ftxA exhibits no apparent homology to hlyC or to other known proteins.

    Techniques Used: Sequencing, Binding Assay, Synthesized

    Sources of the clinical F. alocis strains, isolated and used in the present work, and their respective ftxA and ldh genotypes.
    Figure Legend Snippet: Sources of the clinical F. alocis strains, isolated and used in the present work, and their respective ftxA and ldh genotypes.

    Techniques Used: Isolation

    Phylogenetic relationships among the ten F. alocis strains, based on multilocus sequence typing (MLST) analysis as described in Materials and Methods. The tree with the highest log likelihood is shown. The percentages of trees in which the associated strains clustered together is shown next to the branches. The tree is drawn to scale, with branch lengths measured in the number of substitutions per site. The ftxA and ldh genotypes, respectively, are indicated.
    Figure Legend Snippet: Phylogenetic relationships among the ten F. alocis strains, based on multilocus sequence typing (MLST) analysis as described in Materials and Methods. The tree with the highest log likelihood is shown. The percentages of trees in which the associated strains clustered together is shown next to the branches. The tree is drawn to scale, with branch lengths measured in the number of substitutions per site. The ftxA and ldh genotypes, respectively, are indicated.

    Techniques Used: Sequencing



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    genome sequenced f alocis type strain  (ATCC)
    96
    ATCC genome sequenced f alocis type strain
    ( A ) Overlapping conserved domains in the FtxA protein sequence, deduced using InterPro. The C-terminal portion displays homology to the Hemolysin-type calcium binding-related domain (IPR010566), and the serralysin-like metalloprotease superfamily (IPR011049), and contains repeats-in-toxins (RTX) calcium-binding nonapeptide repeats (IPR001343), and Hemolysin-type calcium-binding conserved sites (IPR018511). ( B ) One archetypal RTX gene cluster ( hlyCABD ) encodes the E. coli alpha-hemolysin, HlyA. HlyA is synthesized as an inactive protoxin, ProHlyA, which is post-translationally activated in two steps, first via HlyC-directed acylation in the cytoplasm, and then by binding Ca 2+ in the extracellular medium . The cyaE gene of B. pertussis encodes a homologue to E. coli tolC and plays a critical role in the secretion of CyaA . We identified no equivalent to an HlyC-homologue in the F. <t>alocis</t> genomes. The hypothetical protein encoded upstream of ftxA exhibits no apparent homology to hlyC or to other known proteins.
    Genome Sequenced F Alocis Type Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/genome+sequenced+f+alocis+type+strain/pmc07692872-10-9-14?v=ATCC
    Average 96 stars, based on 1 article reviews
    genome sequenced f alocis type strain - by Bioz Stars, 2026-08
    96/100 stars
    		  Buy from Supplier

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    ( A ) Overlapping conserved domains in the FtxA protein sequence, deduced using InterPro. The C-terminal portion displays homology to the Hemolysin-type calcium binding-related domain (IPR010566), and the serralysin-like metalloprotease superfamily (IPR011049), and contains repeats-in-toxins (RTX) calcium-binding nonapeptide repeats (IPR001343), and Hemolysin-type calcium-binding conserved sites (IPR018511). ( B ) One archetypal RTX gene cluster ( hlyCABD ) encodes the E. coli alpha-hemolysin, HlyA. HlyA is synthesized as an inactive protoxin, ProHlyA, which is post-translationally activated in two steps, first via HlyC-directed acylation in the cytoplasm, and then by binding Ca 2+ in the extracellular medium . The cyaE gene of B. pertussis encodes a homologue to E. coli tolC and plays a critical role in the secretion of CyaA . We identified no equivalent to an HlyC-homologue in the F. alocis genomes. The hypothetical protein encoded upstream of ftxA exhibits no apparent homology to hlyC or to other known proteins.

    Journal: Toxins

    Article Title: Phylogenetic Analysis of Filifactor alocis Strains Isolated from Several Oral Infections Identified a Novel RTX Toxin, FtxA

    doi: 10.3390/toxins12110687

    Figure Lengend Snippet: ( A ) Overlapping conserved domains in the FtxA protein sequence, deduced using InterPro. The C-terminal portion displays homology to the Hemolysin-type calcium binding-related domain (IPR010566), and the serralysin-like metalloprotease superfamily (IPR011049), and contains repeats-in-toxins (RTX) calcium-binding nonapeptide repeats (IPR001343), and Hemolysin-type calcium-binding conserved sites (IPR018511). ( B ) One archetypal RTX gene cluster ( hlyCABD ) encodes the E. coli alpha-hemolysin, HlyA. HlyA is synthesized as an inactive protoxin, ProHlyA, which is post-translationally activated in two steps, first via HlyC-directed acylation in the cytoplasm, and then by binding Ca 2+ in the extracellular medium . The cyaE gene of B. pertussis encodes a homologue to E. coli tolC and plays a critical role in the secretion of CyaA . We identified no equivalent to an HlyC-homologue in the F. alocis genomes. The hypothetical protein encoded upstream of ftxA exhibits no apparent homology to hlyC or to other known proteins.

    Article Snippet: We here aimed to perform phylogenetic analysis of a genome-sequenced F. alocis type strain (ATCC 35896; CCUG 47790), as well as nine clinical oral strains that we have independently isolated and sequenced, for identification and deeper characterization of novel genomic elements of virulence in this species.

    Techniques: Sequencing, Binding Assay, Synthesized

    Sources of the clinical F. alocis strains, isolated and used in the present work, and their respective ftxA and ldh genotypes.

    Journal: Toxins

    Article Title: Phylogenetic Analysis of Filifactor alocis Strains Isolated from Several Oral Infections Identified a Novel RTX Toxin, FtxA

    doi: 10.3390/toxins12110687

    Figure Lengend Snippet: Sources of the clinical F. alocis strains, isolated and used in the present work, and their respective ftxA and ldh genotypes.

    Article Snippet: We here aimed to perform phylogenetic analysis of a genome-sequenced F. alocis type strain (ATCC 35896; CCUG 47790), as well as nine clinical oral strains that we have independently isolated and sequenced, for identification and deeper characterization of novel genomic elements of virulence in this species.

    Techniques: Isolation

    Phylogenetic relationships among the ten F. alocis strains, based on multilocus sequence typing (MLST) analysis as described in Materials and Methods. The tree with the highest log likelihood is shown. The percentages of trees in which the associated strains clustered together is shown next to the branches. The tree is drawn to scale, with branch lengths measured in the number of substitutions per site. The ftxA and ldh genotypes, respectively, are indicated.

    Journal: Toxins

    Article Title: Phylogenetic Analysis of Filifactor alocis Strains Isolated from Several Oral Infections Identified a Novel RTX Toxin, FtxA

    doi: 10.3390/toxins12110687

    Figure Lengend Snippet: Phylogenetic relationships among the ten F. alocis strains, based on multilocus sequence typing (MLST) analysis as described in Materials and Methods. The tree with the highest log likelihood is shown. The percentages of trees in which the associated strains clustered together is shown next to the branches. The tree is drawn to scale, with branch lengths measured in the number of substitutions per site. The ftxA and ldh genotypes, respectively, are indicated.

    Article Snippet: We here aimed to perform phylogenetic analysis of a genome-sequenced F. alocis type strain (ATCC 35896; CCUG 47790), as well as nine clinical oral strains that we have independently isolated and sequenced, for identification and deeper characterization of novel genomic elements of virulence in this species.

    Techniques: Sequencing