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3.A.6.2.1
Flagellar protein export system.  Infrequent ATP hydrolysis by the FliI6FliJ ring is sufficient for gate activation, allowing processive translocation of export flagellar protein substrates for efficient flagellar assembly (Minamino et al. 2014). FliO has been identified as a flagellar basal body chaparone protein (Fabiani et al. 2017). The flagellar protein export apparatus switches its substrate specificity when hook length has reached approximately 55 nm, and the hydrophilic C-terminal domain of FlhB is involved in this switching process (Inoue et al. 2019). A positively chargef region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export (Kinoshita et al. 2021).

Accession Number:P0A1L5
Protein Name:FliQ aka FLAQ aka STM1980
Length:89
Molecular Weight:9604.00
Species:Salmonella typhimurium [90371]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate

Cross database links:

RefSeq: NP_460933.1   
Entrez Gene ID: 1253501   
Pfam: PF01313   
BioCyc: STYP99287:STM1980-MONOMER   
KEGG: stm:STM1980   

Gene Ontology

GO:0009425 C:bacterial-type flagellum basal body
GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0009306 P:protein secretion

References (2)

[1] “The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assembly.”  Ohnishi K.et.al.   9324257
[2] “Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.”  McClelland M.et.al.   11677609
Structure:
6F2D     

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTPESVMMMG TEAMKVALAL AAPLLLVALI TGLIISILQA ATQINEMTLS FIPKIVAVFI 
61:	AIIVAGPWML NLLLDYVRTL FSNLPYIIG