Annotations for this protein have been verified by the authors of the corresponding papers



DP00027: Negative regulator of flagellin synthesisFASTA viewXML view

General information
DisProt:DP00027
Name:Negative regulator of flagellin synthesis
Synonym(s):FLGM_SALTY
Anti-sigma-28 factor
FlgM
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P26477
UniGene: 
SwissProt: FLGM_SALTY
TrEMBL:  
NCBI (GI): 120306
Source organism:Salmonella typhimurium
Sequence length:97
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSIDRTSPLK PVSTVQTRET SDTPVQKTRQ EKTSAATSAS VTLSDAQAKL MQPGVSDINM - 60
ERVEALKTAI RNGELKMDTG KIADSLIREA QSYLQSK



Functional narrative    

Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of fliA by directly binding to fliA. The N-terminal domain is essential for export and the C-terminal domain possess the fliA binding site. Belongs to the flgM family.

Region 1: 1-97

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 97
Length:97
Region sequence:

MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINM
ERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK

Modification type: Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein inhibitor
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 6.2; D2O 5 %; General Electric Omega 500 MHz (spectrometer); NaCl 10 mM; NaN3 0.02 %; protein (sample) 10 mM; sodium phosphate (buffer) 10 mM)

References:
  1. Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. "The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28." Nat Struct Biol. 1997; 4(4): 285-91. PubMed: 9095196

Comments:
 



References

  1. Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. "The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28." Nat Struct Biol. 1997; 4(4): 285-91. PubMed: 9095196



Comments


AV 7-29-2010 PubMed: 9095196


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