| 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
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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
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| Functional narrative |
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
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| 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.
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| 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: | Polymerization
Structural mortar
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7; Jasco-600 (spectropolarimeter); path length (cylindrical fused quartz cells) 0.2 cm; phosphate (buffer) 10 mM; NaCl 150 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:
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| 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); path length (cylindrical fused quartz cells) 0.2 cm; phosphate (buffer) 10 mM; NaCl 150 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:
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| 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
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| Comments |
AV (6-17-2010) PubMed: 2810365
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