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Conserved domains on  [gi|446628052|ref|WP_000705398|]
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MULTISPECIES: flagellar biosynthesis anti-sigma factor FlgM [Enterobacteriaceae]

Protein Classification

flagellar biosynthesis anti-sigma factor FlgM( domain architecture ID 10023948)

flagellar biosynthesis anti-sigma factor FlgM binds and inhibits the activity of the transcription factor sigma 28

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FlgM_jcvi TIGR03824
flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the ...
 1-89 1.33e-08

flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the alternative sigma factor sigma(28) FliA. The C-terminus of FlgM contains the sigma(28)-binding domain.


:

Pssm-ID: 274802  Cd Length: 95  Bit Score: 47.72  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628052   1 MKITPTMPGNRPTATTAGSSQPRKSTATTTTTQSADDITQAGLQSAQQTLNDQQE-----SDIDSDKVAQMQAMLASGSL 75
Cdd:TIGR03824  1 MKINGIGPPPVNAALRSTRSQAAAKASAAAAAAAAASGDSVSLSSLAQQLQSLEAalassPDVDAEKVAEIKAAIANGSY 80

                         90
                 ....*....|....
gi 446628052  76 QVDTEQLASDMLSF 89
Cdd:TIGR03824 81 KVDAEKIADKLLDF 94
 
Name Accession Description Interval E-value
FlgM_jcvi TIGR03824
flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the ...
 1-89 1.33e-08

flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the alternative sigma factor sigma(28) FliA. The C-terminus of FlgM contains the sigma(28)-binding domain.


Pssm-ID: 274802  Cd Length: 95  Bit Score: 47.72  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628052   1 MKITPTMPGNRPTATTAGSSQPRKSTATTTTTQSADDITQAGLQSAQQTLNDQQE-----SDIDSDKVAQMQAMLASGSL 75
Cdd:TIGR03824  1 MKINGIGPPPVNAALRSTRSQAAAKASAAAAAAAAASGDSVSLSSLAQQLQSLEAalassPDVDAEKVAEIKAAIANGSY 80

                         90
                 ....*....|....
gi 446628052  76 QVDTEQLASDMLSF 89
Cdd:TIGR03824 81 KVDAEKIADKLLDF 94
FlgM COG2747
Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]; ...
 1-92 1.54e-08

Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility];


Pssm-ID: 442044  Cd Length: 101  Bit Score: 47.75  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628052   1 MKITPTMPGN----RPTATTAGSSQPRKSTATTTTTQSADD---ITQAGlQSAQQTLNDQQESDIDSDKVAQMQAMLASG 73
Cdd:COG2747    1 MKINGTGPLSvtavNPYQKAAATAASAGKAAAAASAAAASDsveLSSAA-KQLQQLEELASSPDIDAERVAEIKQAIANG 79

                         90
                 ....*....|....*....
gi 446628052  74 SLQVDTEQLASDMLSFFQN 92
Cdd:COG2747   80 TYKVDAEKIADKLLAFERE 98
FlgM pfam04316
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ...
 43-87 7.86e-07

Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery.


Pssm-ID: 461260  Cd Length: 54  Bit Score: 42.09  E-value: 7.86e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446628052  43 LQSAQQTLndQQESDIDSDKVAQMQAMLASGSLQVDTEQLASDML 87
Cdd:pfam04316 12 LQKAKQAL--AAAPDVREDKVAELKAAIANGTYKVDAEKIADKLL 54
 
Name Accession Description Interval E-value
FlgM_jcvi TIGR03824
flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the ...
 1-89 1.33e-08

flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the alternative sigma factor sigma(28) FliA. The C-terminus of FlgM contains the sigma(28)-binding domain.


Pssm-ID: 274802  Cd Length: 95  Bit Score: 47.72  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628052   1 MKITPTMPGNRPTATTAGSSQPRKSTATTTTTQSADDITQAGLQSAQQTLNDQQE-----SDIDSDKVAQMQAMLASGSL 75
Cdd:TIGR03824  1 MKINGIGPPPVNAALRSTRSQAAAKASAAAAAAAAASGDSVSLSSLAQQLQSLEAalassPDVDAEKVAEIKAAIANGSY 80

                         90
                 ....*....|....
gi 446628052  76 QVDTEQLASDMLSF 89
Cdd:TIGR03824 81 KVDAEKIADKLLDF 94
FlgM COG2747
Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]; ...
 1-92 1.54e-08

Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility];


Pssm-ID: 442044  Cd Length: 101  Bit Score: 47.75  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628052   1 MKITPTMPGN----RPTATTAGSSQPRKSTATTTTTQSADD---ITQAGlQSAQQTLNDQQESDIDSDKVAQMQAMLASG 73
Cdd:COG2747    1 MKINGTGPLSvtavNPYQKAAATAASAGKAAAAASAAAASDsveLSSAA-KQLQQLEELASSPDIDAERVAEIKQAIANG 79

                         90
                 ....*....|....*....
gi 446628052  74 SLQVDTEQLASDMLSFFQN 92
Cdd:COG2747   80 TYKVDAEKIADKLLAFERE 98
FlgM pfam04316
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ...
 43-87 7.86e-07

Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery.


Pssm-ID: 461260  Cd Length: 54  Bit Score: 42.09  E-value: 7.86e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446628052  43 LQSAQQTLndQQESDIDSDKVAQMQAMLASGSLQVDTEQLASDML 87
Cdd:pfam04316 12 LQKAKQAL--AAAPDVREDKVAELKAAIANGTYKVDAEKIADKLL 54
 
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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