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Conserved domains on  [gi|1820080673|ref|WP_165434639|]
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MULTISPECIES: flagellar assembly protein A [Campylobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FapA_N super family cl48415
Flagellar Assembly Protein A N-terminal region; This entry represents an N-terminal region of ...
 126-272 2.80e-03

Flagellar Assembly Protein A N-terminal region; This entry represents an N-terminal region of the FapA protein and its homologs. This region is found in multiple copies in some proteins. Members of this family include FapA (flagellar assembly protein A) 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.


The actual alignment was detected with superfamily member pfam20250:

Pssm-ID: 466401  Cd Length: 174  Bit Score: 39.11  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820080673 126 LQNIYKKMLKLKFLIGIRifdfKKNLMSFCNQHKNIPlnktiQITVAQGIDPIESQDESLIL--------AYKEKTKNYT 197
Cdd:pfam20250  27 LEEILEALKKAGIVYGID----KEALEKLLEEPKELK-----EVLIARGKPPINGEDARIEFlvdtarerVLKPQEEEDR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820080673 198 IDEK-RSGIIVVDENEVVLKHAKFKQGKEGKDLNLHTLKVLAANENKVKFSCSSAFKqvEQDGYTeYIALKKGYVV 272
Cdd:pfam20250  98 VDFReLGSIISVKPGDVLARKIPPTPGEPGRTVFGEVIPPKPGKDLPLKAGKGTEIS--EEDGNL-LIAAIDGQPV 170
 
Name Accession Description Interval E-value
FapA_N pfam20250
Flagellar Assembly Protein A N-terminal region; This entry represents an N-terminal region of ...
 126-272 2.80e-03

Flagellar Assembly Protein A N-terminal region; This entry represents an N-terminal region of the FapA protein and its homologs. This region is found in multiple copies in some proteins. Members of this family include FapA (flagellar assembly protein A) 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.


Pssm-ID: 466401  Cd Length: 174  Bit Score: 39.11  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820080673 126 LQNIYKKMLKLKFLIGIRifdfKKNLMSFCNQHKNIPlnktiQITVAQGIDPIESQDESLIL--------AYKEKTKNYT 197
Cdd:pfam20250  27 LEEILEALKKAGIVYGID----KEALEKLLEEPKELK-----EVLIARGKPPINGEDARIEFlvdtarerVLKPQEEEDR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820080673 198 IDEK-RSGIIVVDENEVVLKHAKFKQGKEGKDLNLHTLKVLAANENKVKFSCSSAFKqvEQDGYTeYIALKKGYVV 272
Cdd:pfam20250  98 VDFReLGSIISVKPGDVLARKIPPTPGEPGRTVFGEVIPPKPGKDLPLKAGKGTEIS--EEDGNL-LIAAIDGQPV 170
 
Name Accession Description Interval E-value
FapA_N pfam20250
Flagellar Assembly Protein A N-terminal region; This entry represents an N-terminal region of ...
 126-272 2.80e-03

Flagellar Assembly Protein A N-terminal region; This entry represents an N-terminal region of the FapA protein and its homologs. This region is found in multiple copies in some proteins. Members of this family include FapA (flagellar assembly protein A) 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.


Pssm-ID: 466401  Cd Length: 174  Bit Score: 39.11  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820080673 126 LQNIYKKMLKLKFLIGIRifdfKKNLMSFCNQHKNIPlnktiQITVAQGIDPIESQDESLIL--------AYKEKTKNYT 197
Cdd:pfam20250  27 LEEILEALKKAGIVYGID----KEALEKLLEEPKELK-----EVLIARGKPPINGEDARIEFlvdtarerVLKPQEEEDR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820080673 198 IDEK-RSGIIVVDENEVVLKHAKFKQGKEGKDLNLHTLKVLAANENKVKFSCSSAFKqvEQDGYTeYIALKKGYVV 272
Cdd:pfam20250  98 VDFReLGSIISVKPGDVLARKIPPTPGEPGRTVFGEVIPPKPGKDLPLKAGKGTEIS--EEDGNL-LIAAIDGQPV 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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