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.
|
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:
- 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)
- Sensitivity to proteolysis (298 K; pH: 7.8; protein (sample) 1 mg/mL; protein-enzyme ratio 300:1 (w/w); proteolytic enzyme (trypsin))
| References:
- 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:
- 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)
- Sensitivity to proteolysis (298 K; pH: 7.8; protein (sample) 1 mg/mL; proteolytic enzyme 200 uL; Tris-HCl (buffer) 20 mM)
| References:
- 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 |
- 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
|