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Literature summary for 2.7.13.3 extracted from

  • Nishikawa, K.; Duncan, M.J.
    Histidine kinase-mediated production and autoassembly of Porphyromonas gingivalis fimbriae (2010), J. Bacteriol., 192, 1975-1987.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Cloned(Commentary)

Cloned (Comment) Organism
gene fimS, DNA and amino acid sequence determination and analysis, the transcriptional start site of fimS is disrupted in strain W83 Porphyromonas gingivalis
gene PGN_0904 or fimS, DNA and amino acid sequence determination and analysis, recombinant expression in the enzyme-deficient Porphyromonas gingivalis strain W38, complementation of the fimS variant in trans, strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface Porphyromonas gingivalis

Protein Variants

Protein Variants Comment Organism
additional information enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS Porphyromonas gingivalis

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
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Porphyromonas gingivalis B2RJ78
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Porphyromonas gingivalis ATCC 33277 B2RJ78
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Porphyromonas gingivalis W83
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-

Synonyms

Synonyms Comment Organism
33277 FimS
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 Porphyromonas gingivalis
FimS
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 Porphyromonas gingivalis
FimS histidine kinase
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 Porphyromonas gingivalis
PGN_0904
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 Porphyromonas gingivalis
W83 FimS
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 Porphyromonas gingivalis

General Information

General Information Comment Organism
evolution different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83 Porphyromonas gingivalis
evolution different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83. Although the production of FimR in W83 is modest, the protein still is detectable and can be functional because its amino acid sequence is almost identical to that of strain ATCC 33277, except for the alteration of one residue from serine to threonine, S209T Porphyromonas gingivalis
malfunction enzyme FimS from W83 is malfunctional. Complementation analysis with chimeric fimS constructs reveals that W83 FimS has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. But even the fimbria-deficient strain W83 retains the ability to polymerize FimA from strain ATCC 33277, indicating the assembly of mature FimA by a primary structure-dependent mechanism. Strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface Porphyromonas gingivalis
physiological function the FimA-related gene cluster (the fim gene cluster) is positively regulated by the FimS-FimR two-component system. The assembly of mature FimA by a primary structure-dependent mechanism. FimSR is the unique and universal regulatory system that activates the fim gene cluster in a fimA genotype-independent manner Porphyromonas gingivalis