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Conserved domains on  [gi|515628088|ref|WP_017060688|]
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MULTISPECIES: flagellar protein FliT [Vibrio]

Protein Classification

flagellar protein FliT( domain architecture ID 10526792)

flagellar biosynthesis protein FliT acts as a substrate-specific chaperone that protects its substrate (FliD) from degradation and aggregation in the cytoplasm and efficiently transfers the substrate to the export apparatus

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FliT pfam05400
Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The ...
27-97 9.65e-03

Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The flagellar proteins FlgN and FliT have been proposed to act as substrate specific export chaperones, facilitating incorporation of the enterobacterial hook-associated axial proteins (HAPs) FlgK/FlgL and FliD into the growing flagellum. In Salmonella typhimurium flgN and fliT mutants, the export of target HAPs is reduced, concomitant with loss of unincorporated flagellin into the surrounding medium.


:

Pssm-ID: 461640  Cd Length: 86  Bit Score: 32.30  E-value: 9.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515628088   27 EEITQLVDNREQLLQNVLQIIDSHPDVKQSSEWFEAITRT-----RKLVELMQSETSRVGKTLHKYRHGAKSVQQY 97
Cdd:pfam05400  11 DELVALEAERQQLVERLRELEPEAPLSDAERAEKRELLRRilendAEIRALLQPRLDELQKLLGQARRQRKANNAY 86
 
Name Accession Description Interval E-value
FliT pfam05400
Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The ...
27-97 9.65e-03

Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The flagellar proteins FlgN and FliT have been proposed to act as substrate specific export chaperones, facilitating incorporation of the enterobacterial hook-associated axial proteins (HAPs) FlgK/FlgL and FliD into the growing flagellum. In Salmonella typhimurium flgN and fliT mutants, the export of target HAPs is reduced, concomitant with loss of unincorporated flagellin into the surrounding medium.


Pssm-ID: 461640  Cd Length: 86  Bit Score: 32.30  E-value: 9.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515628088   27 EEITQLVDNREQLLQNVLQIIDSHPDVKQSSEWFEAITRT-----RKLVELMQSETSRVGKTLHKYRHGAKSVQQY 97
Cdd:pfam05400  11 DELVALEAERQQLVERLRELEPEAPLSDAERAEKRELLRRilendAEIRALLQPRLDELQKLLGQARRQRKANNAY 86
 
Name Accession Description Interval E-value
FliT pfam05400
Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The ...
27-97 9.65e-03

Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The flagellar proteins FlgN and FliT have been proposed to act as substrate specific export chaperones, facilitating incorporation of the enterobacterial hook-associated axial proteins (HAPs) FlgK/FlgL and FliD into the growing flagellum. In Salmonella typhimurium flgN and fliT mutants, the export of target HAPs is reduced, concomitant with loss of unincorporated flagellin into the surrounding medium.


Pssm-ID: 461640  Cd Length: 86  Bit Score: 32.30  E-value: 9.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515628088   27 EEITQLVDNREQLLQNVLQIIDSHPDVKQSSEWFEAITRT-----RKLVELMQSETSRVGKTLHKYRHGAKSVQQY 97
Cdd:pfam05400  11 DELVALEAERQQLVERLRELEPEAPLSDAERAEKRELLRRilendAEIRALLQPRLDELQKLLGQARRQRKANNAY 86
 
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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