RecName: Full=33 kDa chaperonin; AltName: Full=Heat shock protein 33 h - Protein

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Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone. [J Biol Chem. 2010]
Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.
Cremers CM, Reichmann D, Hausmann J, Ilbert M, Jakob U. J Biol Chem. 2010 Apr 9; 285(15):11243-51. Epub 2010 Feb 5.
Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement. [Microb Biotechnol. 2018]
Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement.
Borriss R, Danchin A, Harwood CR, Médigue C, Rocha EPC, Sekowska A, Vallenet D. Microb Biotechnol. 2018 Jan; 11(1):3-17.
An updated metabolic view of the Bacillus subtilis 168 genome. [Microbiology (Reading). 2013]
An updated metabolic view of the Bacillus subtilis 168 genome.
Belda E, Sekowska A, Le Fèvre F, Morgat A, Mornico D, Ouzounis C, Vallenet D, Médigue C, Danchin A. Microbiology (Reading). 2013 Apr; 159(Pt 4):757-770. Epub 2013 Feb 21.

RefSeq protein
See the reference protein sequence for disulfide bond chaperone (heat shock protein HSP33) (NP_387952.1).

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MODBASE, Database of Comparative Protein Structure Models (Sali Lab/UCSF) [MODBASE, Database of Comparat...]
MODBASE, Database of Comparative Protein Structure Models (Sali Lab/UCSF)
Transcript/Protein Information [PANTHER Classification System]
Transcript/Protein Information
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Evolutionary Trace of Functional Site [Evolutionary Trace of Functio...]
Evolutionary Trace of Functional Site

RecName: Full=33 kDa chaperonin; AltName: Full=Heat shock protein 33 homolog; Sh...
RecName: Full=33 kDa chaperonin; AltName: Full=Heat shock protein 33 homolog; Short=HSP33
gi|586894|sp|P37565.1|HSLO_BACSU

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