flagellar motor switch protein FliM is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring) located at the base of the basal body
flagellar motor switch protein FliM; Members of this family are the flagellar motor switch ...
3-319
2.11e-134
flagellar motor switch protein FliM; Members of this family are the flagellar motor switch protein FliM. The family excludes FliM homologs that lack an N-terminal region critical to interaction with phosphorylated CheY. One set lacking this N-terminal region is found in Rhizobium meliloti, in which the direction of flagellar rotation is not reversible (i.e. the FliM homolog does not act to reverse the motor direction), and in related species. Another is found in Buchnera, an obligate intracellular endosymbiont with genes for many of the components of the flagellar apparatus, but not, apparently, for flagellin iself. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 130464 [Multi-domain] Cd Length: 320 Bit Score: 385.52 E-value: 2.11e-134
flagellar protein FliM; This family contains bacterial flagellar protein FliM which is ...
47-227
9.68e-74
flagellar protein FliM; This family contains bacterial flagellar protein FliM which is localized in the flagellar switch complex along with FliG and FliY; all are present in many copies, and together they correspond structurally to the C-ring of the flagellar basal body. FliM does not contain the CheC consensus sequence of the phosphatase active site ([DS]xxxExxNx(22)P) and is not a CheY-P phosphatase. FliM sits in the center of the rotor with the N-terminal region interacting with the signaling protein, phosphorylated CheY (CheY-P). The activated form of CheY destabilizes the parallel arrangement of FliM molecules, and perturbs FliG alignment in a process that may reflect the onset of rotation switching. This suggests a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly. Recent data show that binding of FliM to spermine synthase, SpeE, contributes to flagellar motility, an association that is unique to Helicobacter species.
Pssm-ID: 381736 Cd Length: 181 Bit Score: 225.86 E-value: 9.68e-74
flagellar motor switch protein FliM; Members of this family are the flagellar motor switch ...
3-319
2.11e-134
flagellar motor switch protein FliM; Members of this family are the flagellar motor switch protein FliM. The family excludes FliM homologs that lack an N-terminal region critical to interaction with phosphorylated CheY. One set lacking this N-terminal region is found in Rhizobium meliloti, in which the direction of flagellar rotation is not reversible (i.e. the FliM homolog does not act to reverse the motor direction), and in related species. Another is found in Buchnera, an obligate intracellular endosymbiont with genes for many of the components of the flagellar apparatus, but not, apparently, for flagellin iself. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 130464 [Multi-domain] Cd Length: 320 Bit Score: 385.52 E-value: 2.11e-134
flagellar protein FliM; This family contains bacterial flagellar protein FliM which is ...
47-227
9.68e-74
flagellar protein FliM; This family contains bacterial flagellar protein FliM which is localized in the flagellar switch complex along with FliG and FliY; all are present in many copies, and together they correspond structurally to the C-ring of the flagellar basal body. FliM does not contain the CheC consensus sequence of the phosphatase active site ([DS]xxxExxNx(22)P) and is not a CheY-P phosphatase. FliM sits in the center of the rotor with the N-terminal region interacting with the signaling protein, phosphorylated CheY (CheY-P). The activated form of CheY destabilizes the parallel arrangement of FliM molecules, and perturbs FliG alignment in a process that may reflect the onset of rotation switching. This suggests a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly. Recent data show that binding of FliM to spermine synthase, SpeE, contributes to flagellar motility, an association that is unique to Helicobacter species.
Pssm-ID: 381736 Cd Length: 181 Bit Score: 225.86 E-value: 9.68e-74
Type III flagellar switch regulator (C-ring) FliN C-term; This family includes the C-terminal ...
257-320
3.54e-12
Type III flagellar switch regulator (C-ring) FliN C-term; This family includes the C-terminal region of flagellar motor switch proteins FliN and FliM. It is associated with family FliM, pfam02154 and family FliN_N pfam16973.
Pssm-ID: 460043 [Multi-domain] Cd Length: 66 Bit Score: 60.82 E-value: 3.54e-12
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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