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



DP00026: FlagellinFASTA viewXML view

General information
DisProt:DP00026
Name:Flagellin
Synonym(s):FLIC_SALTY
Phase-1-I flagellin
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P06179
UniGene: 
SwissProt: FLIC_SALTY
TrEMBL:  
NCBI (GI): 20141325
Source organism:Salmonella typhimurium
Sequence length:494
Percent disordered:21%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
AQVINTNSLS LLTQNNLNKS QSALGTAIER LSSGLRINSA KDDAAGQAIA NRFTANIKGL - 60
TQASRNANDG ISIAQTTEGA LNEINNNLQR VRELAVQSAN STNSQSDLDS IQAEITQRLN - 120
EIDRVSGQTQ FNGVKVLAQD NTLTIQVGAN DGETIDIDLK QINSQTLGLD TLNVQQKYKV - 180
SDTAATVTGY ADTTIALDNS TFKASATGLG GTDQKIDGDL KFDDTTGKYY AKVTVTGGTG - 240
KDGYYEVSVD KTNGEVTLAG GATSPLTGGL PATATEDVKN VQVANADLTE AKAALTAAGV - 300
TGTASVVKMS YTDNNGKTID GGLAVKVGDD YYSATQNKDG SISINTTKYT ADDGTSKTAL - 360
NKLGGADGKT EVVSIGGKTY AASKAEGHNF KAQPDLAEAA ATTTENPLQK IDAALAQVDT - 420
LRSDLGAVQN RFNSAITNLG NTVNNLTSAR SRIEDSDYAT EVSNMSRAQI LQQAGTSVLA - 480
QANQVPQNVL SLLR



Functional narrative    

Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Region 1: 1-65 Region 2: 455-494

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:N-terminal
Location:1 - 65
Length:65
Region sequence:

AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGL
TQASR

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Structural mortar
Polymerization
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7; Jasco-600 (spectropolarimeter); NaCl 150 mM; path length (cylindrical fused quartz cells) 0.2 cm; phosphate (buffer) 10 mM)

  2. Sensitivity to proteolysis (298 K; pH: 7.8; protein (sample) 1 mg/mL; protein-enzyme ratio 300:1 (w/w); proteolytic enzyme (trypsin))

References:
  1. Vonderviszt F, Kanto S, Aizawa S, Namba K. "Terminal regions of flagellin are disordered in solution." J Mol Biol. 1989; 209(1): 127-33. PubMed: 2810365

Comments:
 



Region 2
Type:Disordered
Name:C-terminal
Location:455 - 494
Length:40
Region sequence:

DSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Structural mortar
Polymerization
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7; Jasco-600 (spectropolarimeter); NaCl 150 mM; path length (cylindrical fused quartz cells) 0.2 cm; phosphate (buffer) 10 mM)

  2. Sensitivity to proteolysis (298 K; pH: 7.8; protein (sample) 1 mg/mL; proteolytic enzyme 200 uL; Tris-HCl (buffer) 20 mM)

References:
  1. Vonderviszt F, Kanto S, Aizawa S, Namba K. "Terminal regions of flagellin are disordered in solution." J Mol Biol. 1989; 209(1): 127-33. PubMed: 2810365

Comments:
 



References

  1. Vonderviszt F, Kanto S, Aizawa S, Namba K. "Terminal regions of flagellin are disordered in solution." J Mol Biol. 1989; 209(1): 127-33. PubMed: 2810365



Comments


AV (6-17-2010) PubMed: 2810365


If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us.


Disprot-footer
Contact us