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flagellar assembly protein A
This entry represents an N-terminal region of the FapA protein and its homologues. This region is found in multiple copies in some proteins such as Swiss:Q1NVZ6. Members of this family include FapA (flagellar assembly protein A) Swiss:Q7MBR0 found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction [1]. [1]. 27218601. Glucose induces delocalization of a flagellar biosynthesis protein from the flagellated pole. Park S, Park YH, Lee CR, Kim YR, Seok YJ;. Mol Microbiol. 2016;101:795-808. (from Pfam)
FapA family protein
This entry represents the C-terminal beta solenoid domain of FapA and its homologues. Members of this family include FapA (flagellar assembly protein A) Swiss:Q7MBR0 found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction [1]. This entry shows similarity to Pfam:PF03775 suggesting a similar functional role. [1]. 27218601. Glucose induces delocalization of a flagellar biosynthesis protein from the flagellated pole. Park S, Park YH, Lee CR, Kim YR, Seok YJ;. Mol Microbiol. 2016;101:795-808. (from Pfam)
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